X-ray Crystallographic Characterization of the Co(II)-substituted Tris-bound Form of the Aminopeptidase from Aeromonas proteolytica

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Format of Original

9 p.

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Source Publication

Journal of Inorganic Biochemistry

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Original Item ID

doi: 10.1016/j.jinorgbio.2007.03.010


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.


Journal of Inorganic Biochemistry, Vol. 101, No. 8 (August 2007): 1099-1107. DOI.

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.