1LOK

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

Summary for 1LOK

• Entry DOI: 10.2210/pdb1lok/pdb
• Related: 1AMP 1FT7
• Descriptor: Bacterial leucyl aminopeptidase, ZINC ION, SODIUM ION, ... (6 entities in total)
• Functional Keywords: metalloenzyme, aminopeptidase, tris, high resolution, metal coordination, hydrolase
• Biological source: Vibrio proteolyticus
• Total number of polymer chains: 1
• Total formula weight: 31761.38

Authors

Desmarais, W.T.,Bienvenue, D.L.,Bzymek, K.P.,Holz, R.C.,Petsko, G.A.,Ringe, D. (deposition date: 2002-05-06, release date: 2002-11-27, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.2 Å)