Literature DB >> 16260182

Structural biology of mycobacterial proteins: the Bangalore effort.

M Vijayan1.   

Abstract

As part of an international effort and a national programme, structural analysis of mycobacterial proteins involved in recombination and repair, stringent response and protein synthesis has been undertaken, and work on proteins in a couple of metabolic pathways has been initiated. Already X-ray analysed are Mycobacterium tuberculosis and Mycobacterium smegmatis RecA and their nucleotide complexes, and different crystal forms of M. tuberculosis single-stranded DNA binding protein, M. smegmatis DNA binding protein from stationary phase cells and M. tuberculosis ribosome recycling factor. A comparative study involving these structures and those of similar proteins from other sources brings out the special features of the mycobacterial proteins, which are likely to be useful in selective inhibitor design. The structures provide insights into the plasticity of the molecules and its biological implications, and yield valuable information on their assembly and quaternary structure. They also provide leads for further structural investigations.

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Year:  2005        PMID: 16260182     DOI: 10.1016/j.tube.2005.08.011

Source DB:  PubMed          Journal:  Tuberculosis (Edinb)        ISSN: 1472-9792            Impact factor:   3.131


  12 in total

1.  Cloning, expression, purification, crystallization and preliminary X-ray studies of a secreted lectin (Rv1419) from Mycobacterium tuberculosis.

Authors:  Dhabaleswar Patra; R Srikalaivani; Ashish Misra; D D Singh; M Selvaraj; M Vijayan
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2010-11-27

2.  Cloning, expression, purification, crystallization and preliminary X-ray studies of argininosuccinate lyase (Rv1659) from Mycobacterium tuberculosis.

Authors:  A Paul; A Mishra; A Surolia; M Vijayan
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-11-29

3.  Cloning, expression, purification, crystallization and preliminary X-ray studies of the mannose-binding lectin domain of MSMEG_3662 from Mycobacterium smegmatis.

Authors:  Dhabaleswar Patra; Alok Sharma; Divya Chandran; Mamannamana Vijayan
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2011-04-28

4.  Crystallization and preliminary X-ray studies of MutT1 (MSMEG_2390) from Mycobacterium smegmatis.

Authors:  S M Arif; A G Patil; U Varshney; M Vijayan
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2012-09-26

5.  Crowding, molecular volume and plasticity: an assessment involving crystallography, NMR and simulations.

Authors:  M Selvaraj; Rais Ahmad; Umesh Varshney; M Vijayan
Journal:  J Biosci       Date:  2012-12       Impact factor: 1.826

6.  Crystallization and preliminary X-ray characterization of MutT2, MSMEG_5148 from Mycobacterium smegmatis.

Authors:  S M Arif; P B Sang; U Varshney; M Vijayan
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2014-01-21       Impact factor: 1.056

7.  Structural studies on Mycobacterium tuberculosis RecA: molecular plasticity and interspecies variability.

Authors:  Anu V Chandran; J Rajan Prabu; Astha Nautiyal; K Neelakanteshwar Patil; K Muniyappa; M Vijayan
Journal:  J Biosci       Date:  2015-03       Impact factor: 1.826

8.  Preexisting variation in DNA damage response predicts the fate of single mycobacteria under stress.

Authors:  Giulia Manina; Anna Griego; Lalit Kumar Singh; John D McKinney; Neeraj Dhar
Journal:  EMBO J       Date:  2019-10-04       Impact factor: 11.598

9.  Molecular flexibility of Mycobacterium tuberculosis ribosome recycling factor and its functional consequences: an exploration involving mutants.

Authors:  M Selvaraj; A Govindan; A Seshadri; B Dubey; U Varshney; M Vijayan
Journal:  J Biosci       Date:  2013-12       Impact factor: 1.826

10.  Structural Insights into ribosome recycling factor interactions with the 70S ribosome.

Authors:  Raj D Pai; Wen Zhang; Barbara S Schuwirth; Go Hirokawa; Hideko Kaji; Akira Kaji; Jamie H D Cate
Journal:  J Mol Biol       Date:  2008-01-03       Impact factor: 5.469

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