2prq
From Proteopedia
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'''X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica''' | '''X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica''' | ||
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[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
[[Category: Stamper, C C.]] | [[Category: Stamper, C C.]] | ||
| - | [[Category: | + | [[Category: Aminohydrolase]] |
| - | [[Category: | + | [[Category: Cobalt]] |
| - | [[Category: | + | [[Category: Metalloprotease]] |
| - | [[Category: | + | [[Category: Peptidase]] |
| - | [[Category: | + | [[Category: Tri]] |
| - | [[Category: | + | [[Category: X-ray]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:41:22 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:41, 4 May 2008
X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica
Overview
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.
About this Structure
2PRQ is a Single protein structure of sequence from Vibrio proteolyticus. Full crystallographic information is available from OCA.
Reference
X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica., Munih P, Moulin A, Stamper CC, Bennett B, Ringe D, Petsko GA, Holz RC, J Inorg Biochem. 2007 Aug;101(8):1099-107. Epub 2007 Apr 11. PMID:17574677 Page seeded by OCA on Sun May 4 13:41:22 2008
