2DEA
Crystal Structure of the Aminopeptidase of Aeromonas proteolytica at pH 4.7
Summary for 2DEA
| Entry DOI | 10.2210/pdb2dea/pdb |
| Related | 1FT7 1LOK 1RTQ 1TXR |
| Descriptor | Bacterial leucyl aminopeptidase, ZINC ION, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | aminopeptidase, metalloenzyme, bimetalloenzyme, low ph, zinc enzyme, hydrolase |
| Biological source | Vibrio proteolyticus |
| Cellular location | Secreted: Q01693 |
| Total number of polymer chains | 1 |
| Total formula weight | 32391.96 |
| Authors | Petsko, G.A.,Ringe, D.,Desmarais, W. (deposition date: 2006-02-10, release date: 2006-07-25, Last modification date: 2024-10-30) |
| Primary citation | Desmarais, W.,Bienvenue, D.L.,Bzymek, K.P.,Petsko, G.A.,Ringe, D.,Holz, R.C. The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica. J.Biol.Inorg.Chem., 11:398-408, 2006 Cited by PubMed Abstract: 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. PubMed: 16596389DOI: 10.1007/s00775-006-0093-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.24 Å) |
Structure validation
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