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Vijayan, Mamannamana
- 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
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- Structural variability of Mycobacterium tuberculosis SSB and susceptibility to inhibition
Abstract Views :174 |
PDF Views:80
Authors
Srikalaivani Raja
1,
Anju Paul
1,
Sriram Raghavan
2,
Sibi Narayanan
3,
Somnath Shee
4,
Amit Singh
4,
Umesh Varshney
5,
Balasubramanian Gopal
1,
Mamannamana Vijayan
1
Affiliations
1 Molecular Biophysics Unit, Indian Institute of Science, Bengaluru 560 012, IN
2 Molecular Biophysics Unit, Indian Institute of Science, Bengaluru 560 012, India; Present address: RIKEN Center for Computational Science, JP
3 Molecular Biophysics Unit, Indian Institute of Science, Bengaluru 560 012, India; Present address: Sitaram Ayurveda Private Limited, Thrissur 680 007, IN
4 Department of Microbiology and Cell Biology, Indian Institute of Science, Bengaluru 560 012, India; Centre for Infectious Disease Research, Indian Institute of Science, Bengaluru 560 012, IN
5 Department of Microbiology and Cell Biology, Indian Institute of Science, Bengaluru 560 012, IN
1 Molecular Biophysics Unit, Indian Institute of Science, Bengaluru 560 012, IN
2 Molecular Biophysics Unit, Indian Institute of Science, Bengaluru 560 012, India; Present address: RIKEN Center for Computational Science, JP
3 Molecular Biophysics Unit, Indian Institute of Science, Bengaluru 560 012, India; Present address: Sitaram Ayurveda Private Limited, Thrissur 680 007, IN
4 Department of Microbiology and Cell Biology, Indian Institute of Science, Bengaluru 560 012, India; Centre for Infectious Disease Research, Indian Institute of Science, Bengaluru 560 012, IN
5 Department of Microbiology and Cell Biology, Indian Institute of Science, Bengaluru 560 012, IN
Source
Current Science, Vol 122, No 3 (2022), Pagination: 281-289Abstract
Single-stranded DNA is formed at various stages of DNA metabolism. It is protected from degradation by single-stranded DNA-binding proteins (SSBs). Structural variability has been observed in the quaternary arrangement of tetrameric SSBs from mycobacteria and other sources. Here we describe two novel crystal forms which illustrate the extent of structural variability. Docking studies carried out with inhibitors identified from DNA-binding assays allowed the characterization of eight distinct potential binding regions or grooves on each tetramer that circumvent structurally variable regions. Compounds known to inhibit certain bacterial SSBs were tested against Mycobacterium tuberculosis SSB (MtSSB) using DNA-binding and cellular assays. We report two compounds that inhibit MtSSB and growth of the bacterium. Together, this structural analysis reveals a strategy to exploit the variability of MtSSB for the design of inhibitors to this protein. The variability in structure of MtSSB could contribute to its susceptibility to inhibitionKeywords
Binding regions, crystal structure, docking, inhibitor development, Mycobacterium tuberculosis, structural plasticity.Full Text
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