PMID:17574677
| Citation |
Munih, P, Moulin, A, Stamper, CC, Bennett, B, Ringe, D, Petsko, GA and Holz, RC (2007) X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica. J. Inorg. Biochem. 101:1099-107 |
|---|---|
| Abstract |
The X-ray crystal structure of the Co(II)-loaded form of the aminopeptidase from Aeromonas proteolytica ([CoCo(AAP)]) was solved to 2.2A resolution. [CoCo(AAP)] folds into an alpha/beta globular domain with a twisted beta-sheet hydrophobic core sandwiched between alpha-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 3.3A. 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 1.9A, 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. |
| Links |
PubMed Online version:10.1016/j.jinorgbio.2007.03.010 |
| Keywords |
Aeromonas/enzymology; Aminopeptidases/chemistry; Aminopeptidases/metabolism; Binding Sites; Cobalt/chemistry; Cobalt/metabolism; Crystallization; Crystallography, X-Ray; Hydrogen Bonding; Metalloendopeptidases/chemistry; Metalloendopeptidases/metabolism; Protein Folding; Tromethamine; Zinc/chemistry |
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