2XW7

Structure of Mycobacterium smegmatis putative reductase MS0308

2XW7 の概要

• エントリーDOI: 10.2210/pdb2xw7/pdb
• 分子名称: DIHYDROFOLATE REDUCTASE, TETRAETHYLENE GLYCOL, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, nadph
• 由来する生物種: MYCOBACTERIUM SMEGMATIS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41166.18

構造登録者

Evangelopoulos, D.,Gupta, A.,Lack, N.,Cronin, N.,Daviter, T.,Sim, E.,Keep, N.H.,Bhakta, S. (登録日: 2010-11-01, 公開日: 2010-12-01, 最終更新日: 2024-11-20)

主引用文献

Evangelopoulos, D.,Cronin, N.,Daviter, T.,Sim, E.,Keep, N.H.,Bhakta, S.
Characterization of an Oxidoreductase from the Arylamine N-Acetyltransferase Operon in Mycobacterium Smegmatis.
FEBS J., 278:4824-, 2011

PubMed Abstract: Mycobacterium tuberculosis, the most successful bacterial pathogen, causes tuberculosis, a disease that still causes more than 2 million deaths per year. Arylamine N-acetyltransferase is an enzyme that is conserved in most Mycobacterium spp. The nat gene belongs to an operon that is important for the intracellular survival of M. tuberculosis within macrophages. The nat operon in Mycobacterium smegmatis and other fast-growing mycobacterial species has a unique organization containing genes with uncharacterized function. Here, we describe the biochemical, biophysical and structural characterization of the MSMEG_0308 gene product (MS0308) of the M. smegmatis nat operon. While characterizing the function of MS0308, we validated the oxidoreductase property; however, we found that the enzyme was not utilizing dihydrofolate as its substrate, hence we first report that MS0308 is not a dihydrofolate reductase, as annotated in the genome. The structure of this oxidoreductase was solved at 2.0 Å in complex with the cofactor NADPH and has revealed the hydrophobic pocket where the endogenous substrate binds.

PubMed: 21972977
DOI: 10.1111/J.1742-4658.2011.08382.X

実験手法

X-RAY DIFFRACTION (2 Å)