5AKQ

X-ray structure and mutagenesis studies of the N-isopropylammelide isopropylaminohydrolase, AtzC

5AKQ の概要

• エントリーDOI: 10.2210/pdb5akq/pdb
• 分子名称: N-ISOPROPYLAMMELIDE ISOPROPYL AMIDOHYDROLASE, CHLORIDE ION, ZINC ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, atrazine degradation, enzyme evolution
• 由来する生物種: PSEUDOMONAS SP. ADP
• 細胞内の位置: Cytoplasm : O52063
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94541.01

構造登録者

Balotra, S.,Warden, A.C.,Newman, J.,Briggs, L.J.,Scott, C.,Peat, T.S. (登録日: 2015-03-05, 公開日: 2015-03-18, 最終更新日: 2024-01-10)

主引用文献

Balotra, S.,Warden, A.C.,Newman, J.,Briggs, L.J.,Scott, C.,Peat, T.S.
X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, Atzc
Plos One, 1:37700-, 2015

PubMed Abstract: The N-isopropylammelide isopropylaminohydrolase from Pseudomonas sp. strain ADP, AtzC, provides the third hydrolytic step in the mineralization of s-triazine herbicides, such as atrazine. We obtained the X-ray crystal structure of AtzC at 1.84 Å with a weak inhibitor bound in the active site and then used a combination of in silico docking and site-directed mutagenesis to understand the interactions between AtzC and its substrate, isopropylammelide. The substitution of an active site histidine residue (His249) for an alanine abolished the enzyme's catalytic activity. We propose a plausible catalytic mechanism, consistent with the biochemical and crystallographic data obtained that is similar to that found in carbonic anhydrase and other members of subtype III of the amidohydrolase family.

PubMed: 26390431
DOI: 10.1371/JOURNAL.PONE.0137700

実験手法

X-RAY DIFFRACTION (2.6 Å)