3KLC

Crystal structure of hyperthermophilic nitrilase

3KLC の概要

• エントリーDOI: 10.2210/pdb3klc/pdb
• 関連するPDBエントリー: 3IVZ 3IW3 3KI8
• 分子名称: Beta ureidopropionase (Beta-alanine synthase), BROMIDE ION, ACETIC ACID, ... (5 entities in total)
• 機能のキーワード: alpha-beta sandwich, hydrolase
• 由来する生物種: Pyrococcus abyssi
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60733.60

構造登録者

Raczynska, J.,Vorgias, C.,Antranikian, G.,Rypniewski, W. (登録日: 2009-11-07, 公開日: 2010-11-24, 最終更新日: 2023-09-06)

主引用文献

Raczynska, J.E.,Vorgias, C.E.,Antranikian, G.,Rypniewski, W.
Crystallographic analysis of a thermoactive nitrilase.
J.Struct.Biol., 173:294-302, 2010

PubMed Abstract: The nitrilase superfamily is a large and diverse superfamily of enzymes that catalyse the cleavage of various types of carbon-nitrogen bonds using a Cys-Glu-Lys catalytic triad. Thermoactive nitrilase from Pyrococcus abyssi (PaNit) hydrolyses small aliphatic nitriles like fumaro- and malononitryl. Yet, the biological role of this enzyme is unknown. We have analysed several crystal structures of PaNit: without ligands, with an acetate ion bound in the active site and with a bromide ion in the active site. In addition, docking calculations have been performed for fumaro- and malononitriles. The structures provide a proof for specific binding of the carboxylate ion and a general affinity for negatively changed ligands. The role of residues in the active site is considered and an enzymatic reaction mechanism is proposed in which Cys146 acts as the nucleophile, Glu42 as the general base, Lys113/Glu42 as the general acid, WatA as the hydrolytic water and Nζ_Lys113 and N_Phe147 form the oxyanion hole.

PubMed: 21095228
DOI: 10.1016/j.jsb.2010.11.017

実験手法

X-RAY DIFFRACTION (1.76 Å)