The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica |
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| Authors: | William Desmarais David L. Bienvenue Krzysztof P. Bzymek Gregory A. Petsko Dagmar Ringe Richard C. Holz |
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| Affiliation: | (1) Program in Biophysics and Structural Biology, Brandeis University, 415 South Street, Waltham, MA 02254-9110, USA;(2) The Rosenstiel Basic Medical Sciences Research Center, MS029, Brandeis University, 415 South Street, Waltham, MA 02454-9110, USA;(3) Department of Chemistry, Brandeis University, Waltham, MA 02254-9110, USA;(4) Department of Biochemistry, Brandeis University, Waltham, MA 02254-9110, USA;(5) Department of Chemistry and Biochemistry, Utah State University, Logan, UT 84322-0300, USA |
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| 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.The coordinates for the 0.95-Å resolution structure and the 1.24-Å structure at pH 4.7 were deposited in the RCSB Protein Data Bank and have PDB ID numbers of 1RTQ and 2DEA, respectively. |
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| Keywords: | Crystallization Electronic structure |
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