The High-Resolution Structures of the Neutral and the Low pH Crystals of Aminopeptidase from Aeromonas proteolytica

Authors

William Desmarais, Brandeis University
David L. Bienvenue, Utah State UniversityFollow
Krzysztof P. Bzymek, Utah State University
Gregory A. Petsko, Brandeis University
Dagmar Ringe, Brandeis University
Richard C. Holz, Marquette UniversityFollow

Document Type

Article

Publication Date

4-2006

Source Publication

Journal of Biological Inorganic Chemistry

Source ISSN

0949-8257

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

Accepted version. Journal of Biological Inorganic Chemistry, Vol. 11, No. 4 (April 2006): 398-408. DOI. © 2006 Springer Nature Switzerland AG. Part of Springer Nature. Used with permission.

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

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Recommended Citation

Desmarais, William; Bienvenue, David L.; Bzymek, Krzysztof P.; Petsko, Gregory A.; Ringe, Dagmar; and Holz, Richard C., "The High-Resolution Structures of the Neutral and the Low pH Crystals of Aminopeptidase from Aeromonas proteolytica" (2006). Chemistry Faculty Research and Publications. 333.
https://epublications.marquette.edu/chem_fac/333