4BVS

Cyanuric acid hydrolase: evolutionary innovation by structural concatenation.

「3ZGT」から置き換えられました

4BVS の概要

• エントリーDOI: 10.2210/pdb4bvs/pdb
• 関連するPDBエントリー: 4BVQ 4BVR 4BVT
• 分子名称: CYANURIC ACID AMIDOHYDROLASE, MAGNESIUM ION, 1,3,5-triazine-2,4,6-triamine, ... (4 entities in total)
• 機能のキーワード: hydrolase, amidase
• 由来する生物種: PSEUDOMONAS SP. ADP
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81138.16

構造登録者

Peat, T.S.,Balotra, S.,Wilding, M.,French, N.G.,Briggs, L.J.,Panjikar, S.,Cowieson, N.,Newman, J.,Scott, C. (登録日: 2013-06-28, 公開日: 2013-07-17, 最終更新日: 2023-12-20)

主引用文献

Peat, T.S.,Balotra, S.,Wilding, M.,French, N.G.,Briggs, L.J.,Panjikar, S.,Cowieson, N.,Newman, J.,Scott, C.
Cyanuric Acid Hydrolase: Evolutionary Innovation by Structural Concatenation.
Mol.Microbiol., 88:1149-, 2013

PubMed Abstract: The cyanuric acid hydrolase, AtzD, is the founding member of a newly identified family of ring-opening amidases. We report the first X-ray structure for this family, which is a novel fold (termed the 'Toblerone' fold) that likely evolved via the concatenation of monomers of the trimeric YjgF superfamily and the acquisition of a metal binding site. Structures of AtzD with bound substrate (cyanuric acid) and inhibitors (phosphate, barbituric acid and melamine), along with mutagenesis studies, allowed the identification of the active site. The AtzD monomer, active site and substrate all possess threefold rotational symmetry, to the extent that the active site possesses three potential Ser-Lys catalytic dyads. A single catalytic dyad (Ser85-Lys42) is hypothesized, based on biochemical evidence and crystallographic data. A plausible catalytic mechanism based on these observations is also presented. A comparison with a homology model of the related barbiturase, Bar, was used to infer the active-site residues responsible for substrate specificity, and the phylogeny of the 68 AtzD-like enzymes in the database were analysed in light of this structure-function relationship.

PubMed: 23651355
DOI: 10.1111/MMI.12249

実験手法

X-RAY DIFFRACTION (2.6 Å)