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Surolia, Avadhesha
- Structural Biology of Plant Lectins and Macromolecular Crystallography in India
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1 Molecular Biophysics Unit, Indian Institute of Science, Bengaluru 560 012, IN
1 Molecular Biophysics Unit, Indian Institute of Science, Bengaluru 560 012, IN
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Current Science, Vol 116, No 9 (2019), Pagination: 1490-1505Abstract
Earnest attempts at initiating macromolecular crystallography, which is central to modern biology, started in India in the 1970s. The most important component of the efforts was on plant lectins. The lectin programme was continuously and almost exclusively supported by the Department of Science and Technology, Government of India. Lectins are quintessential carbohydrate-binding proteins and have acquired considerable importance in relation to biological recognition at cell surface. The plant lectin programme at Bengaluru spanned 40 years and was instrumental in making significant contributions to glycobiology. The work has also produced important results pertaining to protein folding, quaternary association and strategies for generating ligand specificities. The role of the lectin programme in mentoring scientists has been important and many of the senior macromolecular crystallographers in the country were initially trained under this programme. Studies on plant lectins led to those on mycobacterial and archeal lectins. The lectin work has also served as a springboard for the initiation of several other long-range programmes which, in addition to yielding important results, have also helped in training scientists, many of whom are again leaders of structural biology in India. Perhaps, majority of macromolecular crystallographers in India are those who have been trained at Bengaluru and their descendants. Particularly in recent years, there has been an influx of scientists trained in other centres, who have added vibrance to the macromolecular crystallography community. The community is now reasonably coherent, with constructive interactions among its members, and with several common programmes and shared facilities.Keywords
Ligand Specificity, Macromolecular Crystallography, Plant Lectins, Protein Folding, Quaternary Association.Full Text
References
- Sharon, N. and Gallagher, J., Glycobiology marches on with a subtle blend of tastes and flavours. Curr. Opin. Struct. Biol., 2007, 17, 495–497.
- Arnaud, J., Audfray, A. and Imberty, A., Binding sugars: from natural lectins to synthetic receptors and engineered neolectins. Chem. Soc. Rev., 2013, 7, 4798–4813.
- Vijayan, M. and Chandra, N. R., Lectins. Curr. Opin. Struct. Biol., 1999, 9, 707–714.
- Pérez, S., Sarkar, A., Rivet, A., Breton, C. and Imberty, A., Glyco3d: a portal for structural glycosciences. Meth. Mol. Biol., 2015, 1273, 241–258; http://glyco3d.cermav.cnrs.fr.
- Chandran, T., Sivaji, N., Surolia, A. and Vijayan, M., Ligand binding and retention in snake gourd seed lectin (SGSL). A crystallographic, thermodynamic and molecular dynamics study. Glycobiology, 2018, 28, 968–977.
- Reeke, G. N., Becker, J. W. and Edelman, G. M., The covalent and three dimensional structure of concanavalin A. IV. Atomic coordinates, hydrogen bonding, and quaternary structure. J. Biol. Chem., 1975, 250, 1525–1547.
- Hardman, K. D. and Ainsworth, C. F., Structure of concanavalin A at 2.4-Ang resolution. Biochemistry, 1972, 11, 4910–4919.
- Wright, C. S., The crystal structure of wheat germ agglutinin at 2.2 Å resolution. J. Mol. Biol., 1977, 111, 439–457.
- Salunke, D. M., Khan, M. I., Surolia, A. and Vijayan, M., Crystallization and preliminary X-ray studies of the anti-T lectin from peanut (Arachis hypogaea). J. Mol. Biol., 1982, 154, 177–178.
- Mande, S. C. et al., Structural studies on peanut lectin. Indian J. Biochem. Biophys., 1988, 25, 166–171.
- Salunke, D. M., Khan, M. I., Surolia, A. and Vijayan, M., Preparation and preliminary X-ray studies of three acidic pH crystal forms of the anti-T lectin from peanut (Arachis hypogaea). FEBS Lett., 1983, l56, 127–129.
- Dhanaraj, V., Patanjali, S. R., Surolia, A. and Vijayan, M., Preparation and preliminary X-ray studies of two crystal forms of the anti-T lectin from jackfruit (Artocarpus integrifolia). J. Mol. Biol., 1988, 203, 1135–1136.
- Banerjee, R., Dhanaraj, V., Mahanta, S. K., Surolia, A. and Vijayan, M., Preparation and X-ray characterization of four new crystal forms of jacalin, a lectin from Artocarpus integrifolia. J. Mol. Biol., 1991, 221, 773–776.
- Sankaranarayanan, R., Puri, K. D., Ganesh, V., Banerjee, R., Surolia, A. and Vijayan, M., Crystallization and preliminary X-ray studies of the basic lectin from winged bean (Psophocarpus tetragonolobus). J. Mol. Biol., 1993, 229, 558–560.
- Banerjee, R. et al., Crystal structure of peanut lectin, a protein with an unusual quaternary structure. Proc. Natl. Acad. Sci. USA, 1994, 91, 227–231.
- Sankaranarayanan, R., Sekar, K., Banerjee, R., Sharma, V., Surolia, A. and Vijayan, M., A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a β -prism fold. Nature Struct. Biol., 1996, 3, 596–603.
- Montfort, W. et al., The three-dimensional structure of ricin at 2.8 A. J. Biol. Chem., 1987, 262, 5398–5403.
- Hester, G., Kaku, H., Goldstein, I. J. and Wright, C. S., Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family. Nature Struct. Biol., 1995, 2, 472–479.
- Goel, M. et al., Crystal structures of the PNA-porphyrin complex in the presence and absence of lactose: mapping the conformational changes on lactose binding, interacting surfaces, and supramolecular aggregations. Biochemistry, 2005, 44, 5588–5596.
- Goel, M., Anuradha, P., Kaur, K. J., Maiya, B. G., Swamy, M. J. and Salunke, D. M., Porphyrin binding to jacalin is facilitated by the inherent plasticity of the carbohydrate-binding site: novel mode of lectin–ligand interaction. Acta Crystallogr., Sect. D, 2004, 60, 281–288.
- Jain, D., Kaur, K. J. and Salunke, D. M., Enhanced binding of a rationally designed peptide ligand of concanavalin A arises from improved geometrical complementarity. Biochemistry, 2001, 40, 12059–12066.
- Goel, M. et al., Functional equality in the absence of structural similarity: an added dimension to molecular mimicry. J. Biol. Chem., 2001, 276, 39277–39281.
- Jain, D., Kaur, K. J. and Salunke, D. M., Plasticity in protein– peptide recognition: crystal structures of two different peptides bound to concanavalin A. Biophys. J., 2001, 80, 2912–2921.
- Jain, D., Kaur, K., Sundaravadivel, B. and Salunke, D. M., Structural and functional consequences of peptide–carbohydrate mimicry: crystal structure of a carbohydrate-mimicking peptide bound to concanavalin A. J. Biol. Chem., 2000, 275, 16098–16102.
- Mikeska, R. et al., Mistletoe lectin I in complex with galactose and lactose reveals distinct sugar-binding properties. Acta Crystallogr., Sect. F, 2005, 1, 17–25.
- Mishra, V. et al., Crystal structure of Himalayan mistletoe ribosomeinactivating protein reveals the presence of a natural inhibitor and a new functionally active sugar-binding site. J. Biol. Chem., 2005, 280, 20712–20721.
- Mishra, V. et al., Structure of a novel ribosome-inactivating protein from a hemi-parasitic plant inhabiting the northwestern Himalayas. Acta Crystallogr., Sect. D, 2004, 60, 2295–2304.
- Bagaria, A., Surendranath, K., Ramagopal, U. A., Ramakumar, S. and Karande, A. A., Structure–function analysis and insights into the reduced toxicity of Abrus precatorius agglutinin I in relation to abrin. J. Biol. Chem., 2006, 281, 34465–34474.
- Sharma, U., Katre, U. V. and Suresh, C. G., Crystal structure of a plant albumin from Cicer arietinum (chickpea) possessing hemopexin fold and hemagglutination activity. Planta, 2015, 241, 1061–1073.
- Rao, K. N., Suresh, C. G., Katre, U. V., Gaikwad, S. M. and Khan, M. I., Two orthorhombic crystal structures of a galactose-specific lectin from Artocarpus hirsuta in complex with methyl-α -Dgalactose. Acta Crystallogr., Sect. D, 2004, 60, 1404–1412.
- Surya, S., Geethanandan, K., Sadasivan, C. and Haridas, M., Gallic acid binding to Spatholobus parviflorus lectin provides insight to its quaternary structure forming. Int. J. Biol. Macromol., 2016, 91, 696–702.
- Surya, S., Abhilash, J., Geethanandan, K., Sadasivan, C. and Haridas, M., A profile of protein–protein interaction: crystal structure of a lectin–lectin complex. Int. J. Biol. Macromol., 2016, 87, 529–536.
- Abhilash, J., Geethanandan, K., Bharath, S. R., Sabu, A., Sadasivan, C. and Haridas, M., The crystal structure of a lectin from Butea monosperma: insight into its glycosylation and binding of ligands. Int. J. Biol. Macromol., 2015, 72, 1376–1383.
- Geethanandan, K., Abhilash, J., Bharath, S. R., Sadasivan, C. and Haridas, M., X-ray structure of a galactose-specific lectin from Spatholobous parviflorous. Int. J. Biol. Macromol., 2011, 49, 992– 998.
- Salunke, D. M., Swamy, M. J., Khan, M. I., Mande, S. C., Surolia, A. and Vijayan, M., Arrangement of subunits in peanut lectin. Rotation function and chemical cross-linking studies. J. Biol. Chem., 1985, 260, 13576–13579.
- Banerjee, R., Das, K., Ravishankar, R., Suguna, K., Surolia, A. and Vijayan, M., Conformation, protein–carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin–lactose complex. J. Mol. Biol., 1996, 259, 281–296.
- Sharma, V., Vijayan, M. and Surolia, A., Imparting exquisite specificity to peanut agglutinin for the tumor-associated Thomsen– Friedenreich antigen by redesign of its combining site. J. Biol. Chem., 1996, 271, 21209–21213.
- Ravishankar, R., Ravindran, M., Suguna, K., Surolia, A. and Vijayan, M., Crystal structure of the peanut lectin–T–antigen complex. Carbohydrate specificity generated by water bridges. Curr. Sci., 1997, 72, 855–861.
- Sharma, V., Srinivas, V. R., Adhikari, P., Vijayan, M. and Surolia, A., Molecular basis of recognition by Gal/GalNAc specific legume lectins: influence of Glu 129 on the specificity of peanut agglutinin (PNA) towards C2-substituents of galactose. Glycobiology, 1998, 10, 1007–1012.
- Ravishankar, R., Surolia, A., Vijayan, M., Lim, S. and Kishi, Y., Preferred conformation of C-lactose at the free and peanut lectin bound states. J. Am. Chem. Soc., 1998, 120, 11297–11303.
- Ravishankar, R., Suguna, K., Surolia, A. and Vijayan, M., Structures of the complexes of peanut lectin with methyl-β -galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins. Acta Crystallogr., Sect. D, 1999, 55, 1375–1382.
- Ravishankar, R., Thomas, C. J., Suguna, K., Surolia, A. and Vijayan, M., Crystal structures of the peanut lectin-lactose complex at acidic pH: retention of unusual quaternary structure, empty and carbohydrate bound combining sites, molecular mimicry and crystal packing directed by interactions at the combining site. Proteins Struct. Funct. Genet., 2001, 43, 260–270.
- Adhikari, P. et al., Mutational analysis at Asn-41 in peanut agglutinin. A residue critical for the binding of the tumor-associated Thomsen-Friedenreich antigen. J. Biol. Chem., 2001, 276, 40734– 40739.
- Pratap, J. V. et al., The combination of molecular dynamics with crystallography for elucidating protein–ligand interactions: a case study involving peanut lectin complexes with T-antigen and lactose. Acta Crystallogr., Sect. D, 2001, 57, 1584–1594.
- Natchiar, S. K. et al., Structural plasticity of peanut lectin: an X-ray analysis involving variation in pH, ligand binding and crystal structure. Acta Crystallogr., Sect. D, 2004, 60, 211–219.
- Natchiar, S. K. et al., Multivalency in lectins – a crystallographic, modelling and light-scattering study involving peanut lectin and a bivalent ligand. Curr. Sci., 2006, 90, 1230–1237.
- Natchiar, S. K., Srinivas, O., Mitra, N., Surolia, A., Jayaraman, N. and Vijayan, M., Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin. Acta Crystallogr., Sect. D, 2006, 62, 1413–1421.
- Natchiar, S. K., Suguna, K., Surolia, A. and Vijayan, M., Peanut agglutinin, a lectin with an unusual quaternary structure and interesting ligand binding properties. Crystallogr. Rev., 2007, 13, 1–26.
- Prabu, M. M. et al., Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 Å resolution. J. Mol. Biol., 1998, 276, 787–796.
- Kulkarni, K. A., Sinha, S., Katiyar, S., Surolia, A., Vijayan, M. and Suguna, K., Structural basis for the specificity of basic winged bean lectin for the Tn-antigen: a crystallographic, thermodynamic and modelling study. FEBS Lett., 2005, 579, 6775–6780.
- Kulkarni, K. A., Katiyar, S., Surolia, A., Vijayan, M. and Suguna, K., Structural basis for the carbohydrate-specificity of basic winged-bean lectin and its differential affinity for Gal and GalNAc. Acta Crystallogr., Sect. D, 2006, 62, 1319–1324.
- Kulkarni, K. A., Katiyar, S., Surolia, A., Vijayan, M. and Suguna, K., Generation of blood group specificity: new insights from structural studies on the complexes of A- and B-reactive saccharides with basic winged bean agglutinin. Proteins Struct. Funct. Genet., 2007, 68, 762–769.
- Kulkarni, K. A., Katiyar, S., Surolia, A., Vijayan, M. and Suguna, K., Structure and sugar-specificity of basic winged-bean lectin: structures of new disaccharide complexes and a comparative study with other known disaccharide complexes of the lectin. Acta Crystallogr., Sect. D, 2008, 64, 730–737.
- Manoj, N., Srinivas, V. R., Surolia, A., Vijayan, M. and Suguna, K., Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin. J. Mol. Biol., 2000, 302, 1129–1137.
- Jeyaprakash, A. A., Srivastav, A., Surolia, A. and Vijayan, M., Structural basis for the carbohydrate specificities of artocarpin: variation in the length of a loop as a strategy for generating ligand specificity. J. Mol. Biol., 2004, 338, 757–770.
- Thamotharan, S. et al., Modification of the sugar specificity of a plant lectin: structural studies on a point mutant of Erythrina corallodendron lectin. Acta Crystallogr., Sect. D, 2011, 67, 218–227.
- Shetty, K. N., Latha, V. L., Rao, R. N., Nadimpalli, S. K. and Suguna, K., Affinity of a galactose-specific legume lectin from Dolichos lablab to adenine revealed by X-ray crystallography. IUBMB Life, 2013, 65, 633–644.
- Jeyaprakash, A. A. et al., Crystal structure of the jacalin–Tantigen complex and a comparative study of lectin–T-antigen complexes. J. Mol. Biol., 2002, 321, 637–645.
- Jeyaprakash, A. A., Katiyar, S., Swaminathan, C. P., Sekar, K., Surolia, A. and Vijayan, M., Structural basis of the carbohydrate specificities of jacalin: an X-ray and modeling study. J. Mol. Biol., 2003, 332, 217–228.
- Jeyaprakash, A. A. et al., Structural basis for the energetics of jacalin–sugar interactions: promiscuity versus specificity. J. Mol. Biol., 2005, 347, 181–188.
- Sharma, A., Sekar, K. and Vijayan, M., Structure, dynamics, and interactions of jacalin. Insights from molecular dynamics simulations examined in conjunction with results of X-ray studies. Proteins Struct. Funct. Bioinformat., 2009, 77, 760–777.
- Abhinav, K. V., Sharma, K., Swaminathan, C. P., Surolia, A. and Vijayan, M., Jacalin-carbohydrate interactions: distortion of the ligand molecule as a determinant of affinity. Acta Crystallogr., Sect. D, 2015, 71, 324–331.
- Abhinav, K. V., Sharma, K., Surolia, A. and Vijayan, M., Effect of linkage on the location of reducing and nonreducing sugars bound to jacalin. IUBMB Life, 2016, 68, 971–979.
- Abhinav, K. V., Sharma, K., Surolia, A. and Vijayan, M., Distortion of the ligand molecule as a strategy for modulating binding affinity: further studies involving complexes of jacalin with β -substituted disaccharides. IUBMB Life, 2017, 69, 72–78.
- Pratap, J. V., Jeyaprakash, A. A., Rani, P. G., Sekar, K., Surolia, A. and Vijayan, M., Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-α -Dmannose: implications to the generation of carbohydrate specificity. J. Mol. Biol., 2002, 317, 237–247.
- Jeyaprakash, A. A., Srivastav, A., Surolia, A. and Vijayan, M., Structural basis for the carbohydrate specificities of artocarpin: variation in the length of a loop as a strategy for generating ligand specificity. J. Mol. Biol., 2004, 338, 757–770.
- Singh, D. D., Saikrishnan, K., Kumar, P., Surolia, A., Sekar, K. and Vijayan, M., Unusual sugar specificity of banana lectin from Musa paradisiaca and its probable evolutionary origin. Crystallographic and modelling studies. Glycobiology, 2005, 15, 1025– 1032.
- Sharma, A. and Vijayan, M., Influence of glycosidic linkage on the nature of carbohydrate binding in β -prism I fold lectins: an X-ray and molecular dynamics investigation on banana lectincarbohydrate complexes. Glycobiology, 2011, 21, 23–33.
- Chandra, N. R., Ramachandraiah, G., Bachhawat, K., Dam, T. K., Surolia, A. and Vijayan, M., Crystal structure of a dimeric mannose-specific agglutinin from garlic: quaternary association and carbohydrate specificity. J. Mol. Biol., 1999, 285, 1157–1168.
- Ramachandraiah, G., Chandra, N. R., Surolia, A. and Vijayan, M., Re-refinement using reprocessed data to improve the quality of the structure: a case study involving garlic lectin. Acta Crystallogr., Sect. D, 2002, 58, 414–420.
- Ramachandraiah, G., Chandra, N. R., Surolia, A. and Vijayan, M., Computational analysis of multivalency in lectins: structures of garlic lectin–oligosaccharide complexes and their aggregates. Glycobiology, 2003, 13, 765–775.
- Shetty, K. N., Bhat, G. G., Inamdar, S. R., Swamy, B. M. and Suguna, K., Crystal structure of a-prism II lectin from Remusatia vivipara. Glycobiology, 2012, 22, 56–69.
- Sharma, A. et al., The sequence and structure of snake gourd (Trichosanthes anguina) seed lectin, a three-chain nontoxic homologue of type II RIPs. Acta Crystallogr., Sect. D, 2013, 69, 1493– 1503.
- Chandran, T., Sharma, A. and Vijayan, M., Structural studies on a non-toxic homologue of type II RIPs from bitter gourd: molecular basis of non-toxicity, conformational selection and glycan structure. J. Biosci., 2015, 40, 929–941.
- Sinha, S., Gupta, G., Vijayan, M. and Surolia, A., Subunit assembly of plant lectins. Curr. Opin. Struct. Biol., 2007, 17, 498–505.
- Abhinav, K. V. and Vijayan, M., Structural diversity and ligand specificity of lectins. The Bangalore effort. J. Macromol. Sci., Part A, 2014, 86, 1335–1355.
- Chandra, N. R., Prabu, M. M., Suguna, K. and Vijayan, M., Structural similarity and functional diversity in proteins containing the legume lectin fold. Protein Eng., 2001, 14, 857–866.
- Chandran, T., Sharma, A. and Vijayan, M., Generation of ligand specificity and modes of oligomerization in beta-prism I fold lectins. Adv. Proteins Chem. Struct. Biol., 2013, 92, 135–178.
- Prabu, M. M., Suguna, K. and Vijayan, M., Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins. Proteins Struct. Funct. Genet., 1999, 35, 58–69.
- Delbaere, L. T. J. et al., Molecular recognition of a human blood group determinant by a plant lectin. Can. J. Chem., 1990, 68, 1116–1121.
- Shaanan, B., Lis, H. and Sharon, N., Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose. Science, 1991, 254, 862–866.
- Schwarz, F. P., Puri, K. and Surolia, A., Thermodynamics of the binding of galactopyranoside derivatives to the basic lectin from winged bean (Psophocarpus tetrogonolobus). J. Biol. Chem., 1991, 266, 24344–24350.
- Surolia, A., Sharon, N. and Schwarz, F. P., Thermodynamics of monosaccharide and disaccharide binding to Erythrina corallodendron lectin. J. Biol. Chem., 1996, 27, 17697–17703.
- Sharma, A. and Vijayan, M., Quaternary association in β -prism I fold plant lectins: insights from X-ray crystallography, modelling and molecular dynamics. J. Biosci., 2011, 36, 793–808.
- Liu, W., Yang, N., Ding, J., Huang, R. H., Hu, Z. and Wang, D. C., Structural mechanism governing the quaternary organization of monocot mannose-binding lectin revealed by the novel monomeric structure of an orchid lectin. J. Biol. Chem., 2005, 280, 14865– 14876.
- Sharma, V. and Surolia, A., Analyses of carbohydrate recognition by legume lectins: size of the combining site loops and their primary specificity. J. Mol. Biol., 1997, 267, 433–445.
- Sharma, A., Chandran, D., Singh, D. D. and Vijayan, M., Multiplicity of carbohydrate-binding sites in beta-prism fold lectins: occurrence and possible evolutionary implications. J. Biosci., 2007, 32, 1089–1110.
- Abhinav, K. V., Sharma, A. and Vijayan, M., Identification of mycobacterial lectins from genomic data. Proteins Struct. Funct. Bioinformat., 2013, 81, 644–657.
- Patra, D., Srikalaivani, R., Misra, A., Singh, D. D., Selvaraj, M. and Vijayan, M., Cloning, expression, purification, crystallization and preliminary X-ray studies of a secreted lectin (Rv1419) from Mycobacterium tuberculosis. Acta Crystallogr., Sect. F, 2010, 66, 1662–1665.
- Patra, D., Sharma, A., Chandran, D. and Vijayan, M., Cloning, expression, purification, crystallization and preliminary X-ray studies of the mannose-binding lectin domain of MSMEG-3662 from Mycobacterium smegmatis. Acta Crystallogr., Sect. F, 2011, 67, 596–599.
- Patra, D., Mishra, P., Vijayan, M. and Surolia, A., Negative cooperativity and high affinity in chitooligosaccharide binding by a Mycobacterium smegmatis protein containing LysM and Lectin domains. Biochemistry, 2016, 55, 49–61.
- Patra, D., Mishra, P., Surolia, A. and Vijayan, M., Structure, interactions and evolutionary implications of a domain-swapped lectin dimer from Mycobacterium smegmatis. Glycobiology, 2014, 24, 956–965.
- Abhinav, K. V., Samuel, E. and Vijayan, M., Archeal lectins: an identification through a genomic search. Proteins Struct. Funct. Bioinformat., 2016, 84, 21–30.
- Sivaji, N., Abhinav, K. V. and Vijayan, M., Crystallization and biochemical characterization of an archaeal lectin from Methanococcus voltae A3. Acta Crystallogr., Sect. F, 2017, F73, 300–304.