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

Anu, V. Chandran and Rajan, Prabu. J and Asha, Nautiyal and Neelakanteshwar Patil, K. (2015) Structural studies on Mycobacterium tuberculosis RecA: Molecular plasticity and interspecies variability. Journal of Biosciences, 40 (1). pp. 13-30. ISSN 0021-8561

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Abstract

Structures of crystals of Mycobacterium tuberculosis RecA, grown and analysed under different conditions, provide insights into hitherto underappreciated details of molecular structure and plasticity. In particular, they yield information on the invariant and variable features of the geometry of the P-loop, whose binding to ATP is central for all the biochemical activities of RecA. The strengths of interaction of the ligands with the P-loop reveal significant differences. This in turn affects the magnitude of the motion of the ‘switch’ residue, Gln195 in M. tuberculosis RecA, which triggers the transmission of ATP-mediated allosteric information to the DNA binding region. M. tuberculosis RecA is substantially rigid compared with its counterparts from M. smegmatis and E. coli, which exhibit concerted internal molecular mobility. The interspecies variability in the plasticity of the two mycobacterial proteins is particularly surprising as they have similar sequence and 3D structure. Details of the interactions of ligands with the protein, characterized in the structures reported here, could be useful for design of inhibitors against M. tuberculosis RecA.

Item Type:	Article
Uncontrolled Keywords:	Homologous recombination; molecular flexibility; Mycobacterial RecA; P-loop; species variation
Subjects:	500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 07 Enzyme Biochemistry
Divisions:	Protein Chemistry and Technology
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	01 Jan 2021 08:25
Last Modified:	01 Jan 2021 08:25
URI:	http://ir.cftri.res.in/id/eprint/14745

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