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Article
The 1.20 Å Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition
Structure
  • William Desmarais, Brandeis University
  • David L. Bienvenue, Utah State University
  • Krzysztof P. Bzymek, Utah State University
  • Richard C. Holz, Marquette University
  • Gregory A. Petsko, Brandeis University
  • Dagmar Ringe, Brandeis University
Document Type
Article
Publication Date
8-1-2002
Disciplines
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

Structure, Vol. 10, No. 8 (August 2002): 1063-1072. 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, Richard C. Holz, et al.. "The 1.20 Å Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition" Structure (2002) ISSN: 0969-2126
Available at: http://works.bepress.com/richard_holz/53/