1CP6

1-BUTANEBORONIC ACID BINDING TO AEROMONAS PROTEOLYTICA AMINOPEPTIDASE

1CP6 の概要

• エントリーDOI: 10.2210/pdb1cp6/pdb
• 分子名称: PROTEIN (AMINOPEPTIDASE), ZINC ION, 1-BUTANE BORONIC ACID, ... (4 entities in total)
• 機能のキーワード: hydrolase, aminopeptidase
• 由来する生物種: Vibrio proteolyticus
• 細胞内の位置: Secreted: Q01693
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31660.11

構造登録者

Depaola, C.C.,Bennett, B.,Holz, R.C.,Ringe, D.,Petsko, G.A. (登録日: 1999-06-08, 公開日: 1999-06-17, 最終更新日: 2024-10-30)

主引用文献

De Paola, C.C.,Bennett, B.,Holz, R.C.,Ringe, D.,Petsko, G.A.
1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development.
Biochemistry, 38:9048-9053, 1999

PubMed Abstract: Hydrolases containing two metal ions connected by a bridging ligand catalyze reactions important in carcinogensis, tissue repair, post-translational modification, control and regulation of biochemical pathways, and protein degradation. The aminopeptidase from Aeromonas proteolytica serves as a paradigm for the study of such bridged bimetallic proteases since its three-dimensional structure is known to very high resolution and its catalytic reaction is amenable to spectroscopic examination. Herein, we report the X-ray crystal structure at 1.9 A resolution of AAP complexed with 1-butaneboronic acid (BuBA). This structure suggests that this complex represents a snapshot of the proteolytic reaction in an arrested form between the Michaelis complex and the transition state. Comparison of the structure with spectroscopic and other data allows us to conclude that the apparently structurally symmetrical dizinc site is actually asymmetric electrostatically.

PubMed: 10413478
DOI: 10.1021/bi9900572

実験手法

X-RAY DIFFRACTION (1.9 Å)