The 1.20 Å Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition

Authors

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

Document Type

Article

Publication Date

8-2002

Source Publication

Structure

Source ISSN

0969-2126

Abstract

The aminopeptidase from Aeromonas proteolytica (AAP) is a bridged bimetallic enzyme that removes the N-terminal amino acid from a peptide chain. To fully understand the metal roles in the reaction pathway of AAP we have solved the 1.20 Å resolution crystal structure of native AAP (PDB ID = 1LOK). The high-quality electron density maps showed a single Tris molecule chelated to the active site Zn²⁺, alternate side chain conformations for some side chains, a sodium ion that mediates a crystal contact, a surface thiocyanate ion, and several potential hydrogen atoms. In addition, the high precision of the atomic positions has led to insight into the protonation states of some of the active site amino acid side chains.

Comments

Accepted version. Structure, Vol. 10, No. 8 (August 2002): 1063-1072. DOI. © 2002 Cell Press. Published by Elsevier Ltd. Used with permission.

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

Recommended Citation

Desmarais, William; Bienvenue, David L.; Bzymek, Krzysztof P.; Holz, Richard C.; Petsko, Gregory A.; and Ringe, Dagmar, "The 1.20 Å Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition" (2002). Chemistry Faculty Research and Publications. 338.
https://epublications.marquette.edu/chem_fac/338