4OQF

Mycobacterium tuberculosis RecA glycerol bound low temperature structure IIB-SR

Summary for 4OQF

• Entry DOI: 10.2210/pdb4oqf/pdb
• Related: 4PO1 4PO9 4POA 4PPF 4PPG 4PPN 4PPQ 4PQF 4PQR 4PQY 4PR0 4PSA 4PSK 4PSV 4PTL
• Descriptor: Protein RecA, GLYCEROL, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: homologous recombination, dna repair, atpase, dna binding protein, 'p-loop containing ntpase' fold, hydrolysis, atp binding
• Biological source: Mycobacterium tuberculosis; More
• Total number of polymer chains: 1
• Total formula weight: 35528.44

Authors

Chandran, A.V.,Prabu, J.R.,Patil, N.K.,Muniyappa, K.,Vijayan, M. (deposition date: 2014-02-09, release date: 2015-03-18, Last modification date: 2023-11-08)

Primary citation

Chandran, A.V.,Prabu, J.R.,Nautiyal, A.,Patil, K.N.,Muniyappa, K.,Vijayan, M.
Structural studies on Mycobacterium tuberculosis RecA: Molecular plasticity and interspecies variability
J.Biosci., 40:13-30, 2015

PubMed 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.

PubMed: 25740138
DOI: 10.1007/s12038-014-9497-x

Experimental method

X-RAY DIFFRACTION (2.8 Å)