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Article
The High-Resolution Structures of the Neutral and the Low pH Crystals of Aminopeptidase from Aeromonas proteolytica
Journal of Biological Inorganic Chemistry
  • William Desmarais, Brandeis University
  • David L. Bienvenue, Utah State University
  • Krzysztof P. Bzymek, Utah State University
  • Gregory A. Petsko, Brandeis University
  • Dagmar Ringe, Brandeis University
  • Richard C. Holz, Marquette University
Document Type
Article
Publication Date
4-1-2006
Disciplines
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-Å resolution at neutral pH and at 1.24-Å 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.
Comments

Journal of Biological Inorganic Chemistry, Vol. 11, No. 4 (April 2006): 398-408. DOI.

Richard Holz was affiliated with the Utah State University at the time of publication.

Citation Information
William Desmarais, David L. Bienvenue, Krzysztof P. Bzymek, Gregory A. Petsko, et al.. "The High-Resolution Structures of the Neutral and the Low pH Crystals of Aminopeptidase from Aeromonas proteolytica" Journal of Biological Inorganic Chemistry (2006) ISSN: 0949-8257
Available at: http://works.bepress.com/richard_holz/96/