1LOK

The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition

1LOK の概要

• エントリーDOI: 10.2210/pdb1lok/pdb
• 関連するPDBエントリー: 1AMP 1FT7
• 分子名称: Bacterial leucyl aminopeptidase, ZINC ION, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: metalloenzyme, aminopeptidase, tris, high resolution, metal coordination, hydrolase
• 由来する生物種: Vibrio proteolyticus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31761.38

構造登録者

Desmarais, W.T.,Bienvenue, D.L.,Bzymek, K.P.,Holz, R.C.,Petsko, G.A.,Ringe, D. (登録日: 2002-05-06, 公開日: 2002-11-27, 最終更新日: 2024-10-30)

主引用文献

Desmarais, W.T.,Bienvenue, D.L.,Bzymek, K.P.,Holz, R.C.,Petsko, G.A.,Ringe, D.
The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris A tale of Buffer Inhibition
Structure, 10:1063-1072, 2002

PubMed Abstract: The aminopeptidase from Aeromonas proteolytica (AAP) is a bridged bimetallic enzyme that removes the N-terminal amino acid from a peptide chain. To fully understand the metal roles in the reaction pathway of AAP we have solved the 1.20 A resolution crystal structure of native AAP (PDB ID = 1LOK). The high-quality electron density maps showed a single Tris molecule chelated to the active site Zn(2+), alternate side chain conformations for some side chains, a sodium ion that mediates a crystal contact, a surface thiocyanate ion, and several potential hydrogen atoms. In addition, the high precision of the atomic positions has led to insight into the protonation states of some of the active site amino acid side chains.

PubMed: 12176384
DOI: 10.1016/S0969-2126(02)00810-9

実験手法

X-RAY DIFFRACTION (1.2 Å)