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Article
X-ray Crystallographic Characterization of the Co(II)-substituted Tris-bound Form of the Aminopeptidase from Aeromonas proteolytica
Journal of Inorganic Biochemistry
  • Petra Munih, Brandeis University
  • Aaron Moulin, Brandeis University
  • Carin Stamper, Brandeis University
  • Brian Bennett, Marquette University
  • Dagmar Ringe, Brandeis University
  • Gregory A. Petsko, Brandeis University
  • Richard C. Holz, Marquette University
Document Type
Article
Language
eng
Format of Original
9 p.
Publication Date
8-1-2007
Publisher
Elsevier
Original Item ID
doi: 10.1016/j.jinorgbio.2007.03.010
Disciplines
Abstract

The X-ray crystal structure of the Co(II)-loaded form of the aminopeptidase from Aeromonas proteolytica ([CoCo(AAP)]) was solved to 2.2 Å resolution. [CoCo(AAP)] folds into an α/β globular domain with a twisted β-sheet hydrophobic core sandwiched between α-helices, identical to [ZnZn(AAP)]. Co(II) binding to AAP does not introduce any major conformational changes to the overall protein structure and the amino acid residues ligated to the dicobalt(II) cluster in [CoCo(AAP)] are the same as those in the native Zn(II)-loaded structure with only minor perturbations in bond lengths. The Co(II)–Co(II) distance is 3.3 Å. Tris(hydroxymethyl)aminomethane (Tris) coordinates to the dinuclear Co(II) active site of AAP with one of the Tris hydroxyl oxygen atoms (O4) forming a single oxygen atom bridge between the two Co(II) ions. This is the only Tris atom coordinated to the metals with Co1–O and Co2–O bonds distances of 2.2 and 1.9 Å, respectively. Each of the Co(II) ions resides in a distorted trigonal bipyramidal geometry. This important structure bridges the gap between previous structural and spectroscopic studies performed on AAP and is discussed in this context.

Comments

Accepted version. Journal of Inorganic Biochemistry, Vol. 101, No. 8 (August 2007): 1099-1107. DOI. © 2007 Elsevier Inc. Used with permission.

Brian Bennett was affiliated with the Medical College of Wisconsin at the time of publication.

Richard Holz was affiliated with the Loyola University of Chicago at the time of publication.

Citation Information
Petra Munih, Aaron Moulin, Carin Stamper, Brian Bennett, et al.. "X-ray Crystallographic Characterization of the Co(II)-substituted Tris-bound Form of the Aminopeptidase from Aeromonas proteolytica" Journal of Inorganic Biochemistry (2007) ISSN: 0162-0134
Available at: http://works.bepress.com/richard_holz/59/