6BUR

Crystal structures of cyanuric acid hydrolase from Moorella thermoacetica complexed with barbituric acid

6BUR の概要

• エントリーDOI: 10.2210/pdb6bur/pdb
• 分子名称: Cyanuric acid amidohydrolase, BARBITURIC ACID, MALONATE ION, ... (5 entities in total)
• 機能のキーワード: cyanuric acid hydrolase, hydrolase
• 由来する生物種: Moorella thermoacetica ATCC 39073
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 154713.31

構造登録者

Shi, K.,Aihara, H. (登録日: 2017-12-11, 公開日: 2019-06-12, 最終更新日: 2023-10-04)

主引用文献

Shi, K.,Cho, S.,Aukema, K.G.,Lee, T.,Bera, A.K.,Seffernick, J.L.,Wackett, L.P.,Aihara, H.
Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis.
Plos One, 14:e0216979-e0216979, 2019

PubMed Abstract: An ancient enzyme family responsible for the catabolism of the prebiotic chemical cyanuric acid (1,3,5-triazine-2,4,6-triol) was recently discovered and is undergoing proliferation in the modern world due to industrial synthesis and dissemination of 1,3,5-triazine compounds. Cyanuric acid has a highly stabilized ring system such that bacteria require a unique enzyme with a novel fold and subtle active site construction to open the ring. Each cyanuric acid hydrolase monomer consists of three isostructural domains that coordinate and activate the three-fold symmetric substrate cyanuric acid for ring opening. We have now solved a series of X-ray structures of an engineered, thermostable cyanuric acid ring-opening enzyme at 1.51 ~ 2.25 Å resolution, including various complexes with the substrate, a tight-binding inhibitor, or an analog of the reaction intermediate. These structures reveal asymmetric interactions between the enzyme and bound ligands, a metal ion binding coupled to conformational changes and substrate binding important for enzyme stability, and distinct roles of the isostructural domains of the enzyme. The multiple conformations of the enzyme observed across a series of structures and corroborating biochemical data suggest importance of the structural dynamics in facilitating the substrate entry and the ring-opening reaction, catalyzed by a conserved Ser-Lys dyad.

PubMed: 31181074
DOI: 10.1371/journal.pone.0216979

実験手法

X-RAY DIFFRACTION (2.18 Å)