1RTQ

The 0.95 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica

Summary for 1RTQ

• Entry DOI: 10.2210/pdb1rtq/pdb
• Related: 1AMP 1CP6 1FT7 1LOK
• Descriptor: Bacterial leucyl aminopeptidase, THIOCYANATE ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: bimetallic, zinc, high resolution, aminopeptidase, hydrolase
• Biological source: Vibrio proteolyticus
• Cellular location: Secreted: Q01693
• Total number of polymer chains: 1
• Total formula weight: 32554.10

Authors

Desmarais, W.,Bienvenue, D.L.,Krzysztof, B.P.,Holz, R.C.,Petsko, G.A.,Ringe, D. (deposition date: 2003-12-10, release date: 2004-02-10, 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

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: 16596389
DOI: 10.1007/s00775-006-0093-x

Experimental method

X-RAY DIFFRACTION (0.95 Å)