2Q28

Crystal structure of oxalyl-coA decarboxylase from Escherichia coli in complex with adenosine-5`-diphosphate

2Q28 の概要

• エントリーDOI: 10.2210/pdb2q28/pdb
• 関連するPDBエントリー: 2Q27 2Q29
• 分子名称: oxalyl-CoA decarboxylase, MAGNESIUM ION, SULFATE ION, ... (8 entities in total)
• 機能のキーワード: lyase; oxalyl-coa decarboxylase; oxalate degradation; thiamine diphosphate, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 123862.43

構造登録者

Werther, T.,Zimmer, A.,Wille, G.,Hubner, G.,Weiss, M.S.,Konig, S. (登録日: 2007-05-26, 公開日: 2008-06-03, 最終更新日: 2024-02-21)

主引用文献

Werther, T.,Zimmer, A.,Wille, G.,Golbik, R.,Weiss, M.S.,Konig, S.
New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli.
Febs J., 277:2628-2640, 2010

PubMed Abstract: The gene yfdU from Escherichia coli encodes a putative oxalyl coenzyme A decarboxylase, a thiamine diphosphate-dependent enzyme that is potentially involved in the degradation of oxalate. The enzyme has been purified to homogeneity. The kinetic constants for conversion of the substrate oxalyl coenzyme A by the enzyme in the absence and presence of the inhibitor coenzyme A, as well as in the absence and presence of the activator adenosine 5'-diphosphate, were determined using a novel continuous optical assay. The effects of these ligands on the solution and crystal structure of the enzyme were studied using small-angle X-ray scattering and X-ray crystal diffraction. Analyses of the obtained crystal structures of the enzyme in complex with the cofactor thiamine diphosphate, the activator adenosine 5'-diphosphate and the inhibitor acetyl coenzyme A, as well as the corresponding solution scattering patterns, allow comparison of the oligomer structures of the enzyme complexes under various experimental conditions, and provide insights into the architecture of substrate and effector binding sites.

PubMed: 20553497
DOI: 10.1111/j.1742-464X.2010.07673.x

実験手法

X-RAY DIFFRACTION (1.74 Å)