2A87

Crystal Structure of M. tuberculosis Thioredoxin reductase

2A87 の概要

• エントリーDOI: 10.2210/pdb2a87/pdb
• 分子名称: Thioredoxin reductase, MAGNESIUM ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: thioredoxin reductase, trxr, fad, nap, nma, tls, oxidoreductase, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Cytoplasm (By similarity): P52214
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74474.42

構造登録者

Akif, M.,Suhre, K.,Verma, C.,Mande, S.C.,TB Structural Genomics Consortium (TBSGC) (登録日: 2005-07-07, 公開日: 2005-11-29, 最終更新日: 2024-12-25)

主引用文献

Akif, M.,Suhre, K.,Verma, C.,Mande, S.C.
Conformational flexibility of Mycobacterium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis.
Acta Crystallogr.,Sect.D, 61:1603-1611, 2005

PubMed 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.

PubMed: 16301794
DOI: 10.1107/S0907444905030519

実験手法

X-RAY DIFFRACTION (3 Å)