2a87: Difference between revisions

Revision as of 01:30, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2a87.png

Template:STRUCTURE 2a87

Crystal Structure of M. tuberculosis Thioredoxin reductaseCrystal Structure of M. tuberculosis Thioredoxin reductase

Template:ABSTRACT PUBMED 16301794

About this StructureAbout this Structure

2A87 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

ReferenceReference

Conformational flexibility of Mycobacterium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis., Akif M, Suhre K, Verma C, Mande SC, Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1603-11. Epub 2005, Nov 19. PMID:16301794

Page seeded by OCA on Mon Jul 28 01:29:50 2008

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OCA

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-'''Crystal Structure of M. tuberculosis Thioredoxin reductase'''
+===Crystal Structure of M. tuberculosis Thioredoxin reductase===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16301794}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16301794}}
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