Structural highlights
Function
AMPX_VIBPR
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Desmarais W, Bienvenue DL, Bzymek KP, Petsko GA, Ringe D, Holz RC. The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica. J Biol Inorg Chem. 2006 Jun;11(4):398-408. Epub 2006 Apr 5. PMID:16596389 doi:http://dx.doi.org/10.1007/s00775-006-0093-x
