4ADL

Crystal structures of Rv1098c in complex with malate

4ADL の概要

• エントリーDOI: 10.2210/pdb4adl/pdb
• 関連するPDBエントリー: 4ADM 4APA 4APB
• 分子名称: FUMARATE HYDRATASE CLASS II, (2S)-2-hydroxybutanedioic acid (3 entities in total)
• 機能のキーワード: lyase, tricarboxylic acid cycle
• 由来する生物種: MYCOBACTERIUM TUBERCULOSIS
• 細胞内の位置: Cytoplasm (By similarity): O53446
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 211146.44

構造登録者

Mechaly, A.E.,Haouz, A.,Miras, I.,Weber, P.,Shepard, W.,Cole, S.,Alzari, P.M.,Bellinzoni, M. (登録日: 2011-12-26, 公開日: 2012-04-25, 最終更新日: 2023-12-20)

主引用文献

Mechaly, A.E.,Haouz, A.,Miras, I.,Barilone, N.,Weber, P.,Shepard, W.,Alzari, P.M.,Bellinzoni, M.
Conformational Changes Upon Ligand Binding in the Essential Class II Fumarase Rv1098C from Mycobacterium Tuberculosis.
FEBS Lett., 586:1606-, 2012

PubMed Abstract: rv1098c, an essential gene in Mycobacterium tuberculosis, codes for a class II fumarase. We describe here the crystal structure of Rv1098c in complex with l-malate, fumarate or the competitive inhibitor meso-tartrate. The models reveal that substrate binding promotes the closure of the active site through conformational changes involving the catalytic SS-loop and the C-terminal domain, which likely represents a general feature of this enzyme superfamily. Analysis of ligand-enzyme interactions as well as site-directed mutagenesis suggest Ser318 as one of the two acid-base catalysts.

PubMed: 22561013
DOI: 10.1016/J.FEBSLET.2012.04.034

実験手法

X-RAY DIFFRACTION (2.2 Å)