2dea
|
Crystal Structure of the Aminopeptidase of Aeromonas proteolytica at pH 4.7
OverviewOverview
The aminopeptidase from Aeromonas proteolytica (AAP) contains two zinc, ions in the active site and catalyzes the degradation of peptides. Herein, we report the crystal structures of AAP at 0.95-A resolution at neutral pH, and at 1.24-A resolution at low pH. The combination of these structures, allowed the precise modeling of atomic positions, the identification of, the metal bridging oxygen species, and insight into the physical, properties of the metal ions. On the basis of these structures, a new, putative catalytic mechanism is proposed for AAP that is likely relevant, to all binuclear metalloproteases.
About this StructureAbout this Structure
2DEA is a Single protein structure of sequence from Vibrio proteolyticus with ZN and NA as ligands. Active as Bacterial leucyl aminopeptidase, with EC number 3.4.11.10 Full crystallographic information is available from OCA.
ReferenceReference
The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica., Desmarais W, Bienvenue DL, Bzymek KP, Petsko GA, Ringe D, Holz RC, J Biol Inorg Chem. 2006 Jun;11(4):398-408. Epub 2006 Apr 5. PMID:16596389
Page seeded by OCA on Wed Nov 21 09:33:53 2007