1AMP

CRYSTAL STRUCTURE OF AEROMONAS PROTEOLYTICA AMINOPEPTIDASE: A PROTOTYPICAL MEMBER OF THE CO-CATALYTIC ZINC ENZYME FAMILY

Summary for 1AMP

• Entry DOI: 10.2210/pdb1amp/pdb
• Descriptor: AMINOPEPTIDASE, ZINC ION (3 entities in total)
• Functional Keywords: hydrolase(aminopeptidase)
• Biological source: Vibrio proteolyticus
• Cellular location: Secreted: Q01693
• Total number of polymer chains: 1
• Total formula weight: 31558.17

Authors

Chevrier, B.,Schalk, C.,D'Orchymont, H.,Rondeau, J.M.,Moras, D.,Tarnus, C. (deposition date: 1994-04-22, release date: 1994-08-31, Last modification date: 2024-10-30)

Primary citation

Chevrier, B.,Schalk, C.,D'Orchymont, H.,Rondeau, J.M.,Moras, D.,Tarnus, C.
Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family.
Structure, 2:283-291, 1994

PubMed Abstract: Aminopeptidases specifically cleave the amino-terminal residue from polypeptide chains and are involved in the metabolism of biologically active peptides. The family includes zinc-dependent enzymes possessing either one or two zinc ions per active site. Structural studies providing a detailed view of the metal environment may reveal whether the one-zinc and two-zinc enzymes constitute structurally and mechanistically distinct subclasses, and what role the metal ions play in the catalytic process.

PubMed: 8087555
DOI: 10.1016/S0969-2126(00)00030-7

Experimental method

X-RAY DIFFRACTION (1.8 Å)