4J0N

Crystal structure of a manganese dependent isatin hydrolase

4J0N の概要

• エントリーDOI: 10.2210/pdb4j0n/pdb
• 分子名称: Isatin hydrolase B, MANGANESE (II) ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, manganese binding
• 由来する生物種: Labrenzia aggregata IAM 12614
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56382.21

構造登録者

Bjerregaard-Andersen, K.,Sommer, T.,Jensen, J.K.,Jochimsen, B.,Etzerodt, M.,Morth, J.P. (登録日: 2013-01-31, 公開日: 2013-02-20, 最終更新日: 2023-09-20)

主引用文献

Bjerregaard-Andersen, K.,Sommer, T.,Jensen, J.K.,Jochimsen, B.,Etzerodt, M.,Morth, J.P.
A proton wire and water channel revealed in the crystal structure of isatin hydrolase.
J.Biol.Chem., 289:21351-21359, 2014

PubMed Abstract: The high resolution crystal structures of isatin hydrolase from Labrenzia aggregata in the apo and the product state are described. These are the first structures of a functionally characterized metal-dependent hydrolase of this fold. Isatin hydrolase converts isatin to isatinate and belongs to a novel family of metalloenzymes that include the bacterial kynurenine formamidase. The product state, mimicked by bound thioisatinate, reveals a water molecule that bridges the thioisatinate to a proton wire in an adjacent water channel and thus allows the proton released by the reaction to escape only when the product is formed. The functional proton wire present in isatin hydrolase isoform b represents a unique catalytic feature common to all hydrolases is here trapped and visualized for the first time. The local molecular environment required to coordinate thioisatinate allows stronger and more confident identification of orthologous genes encoding isatin hydrolases within the prokaryotic kingdom. The isatin hydrolase orthologues found in human gut bacteria raise the question as to whether the indole-3-acetic acid degradation pathway is present in human gut flora.

PubMed: 24917679
DOI: 10.1074/jbc.M114.568824

実験手法

X-RAY DIFFRACTION (2.25 Å)