The 1.20 A resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: a tale of buffer inhibition. Academic Article uri icon

Overview

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.

publication date

  • August 1, 2002

Research

keywords

  • Aeromonas
  • Aminopeptidases
  • Bacterial Proteins
  • Tromethamine

Identity

Scopus Document Identifier

  • 0036691521

PubMed ID

  • 12176384

Additional Document Info

volume

  • 10

issue

  • 8