Akif, M. and Suhre, K. and Verma, C.S. and Mande, S.C. (2005) Conformational flexibility of Mycobacterium tuberculosisthioredoxin reductase: crystal structure and normal-mode analysis. Acta Crystallographica Section D Biological Crystallography, 61 (12). pp. 1603-1611. ISSN 0907-4449

Preview

Text Acta Cryst D 61 p1603.pdf Download (1102Kb) | Preview

Abstract

The thioredoxin system exists ubiquitously and participates in essential antioxidant and redox-regulation processes via a pair of conserved cysteine residues. In Mycobacterium tuberculosis, which lacks a genuine glutathione system, the thioredoxin system provides reducing equivalents inside the cell. The three-dimensional structure of thioredoxin reductase from M. tuberculosis has been determined at 3 A resolution. TLS refinement reveals a large libration axis, showing that NADPH-binding domain has large anisotropic disorder. The relative rotation of the NADPH domain with respect to the FAD domain is necessary for the thioredoxin reduction cycle, as it brings the spatially distant reacting sites close together. Normal-mode analysis carried out based on the elastic network model shows that the motion required to bring about the functional conformational change can be accounted for by motion along one single mode. TLS refinement and normal-mode analysis thus enhance our understanding of the associated conformational changes.

Item Type:	Article
Depositing User:	Users 2 not found.
Date Deposited:	21 Jul 2015 10:25
Last Modified:	17 Dec 2015 05:10
URI:	http://cdfd.sciencecentral.in/id/eprint/272

Actions (login required)

View Item