2prq: Difference between revisions

Revision as of 19:32, 21 February 2008

X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica

OverviewOverview

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 StructureAbout this Structure

2PRQ is a Single protein structure of sequence from Vibrio proteolyticus with and as ligands. Active as Bacterial leucyl aminopeptidase, with EC number 3.4.11.10 Full crystallographic information is available from OCA.

ReferenceReference

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

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 ==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.
+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==
@@ Line 10: / Line 10: @@
 ==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):1099-1107. Epub 2007 Apr 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17574677 17574677]
+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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17574677 17574677]
 [[Category: Bacterial leucyl aminopeptidase]]
 [[Category: Single protein]]
 [[Category: Vibrio proteolyticus]]
 [[Category: Bennet, B.]]
-[[Category: Holz, R.C.]]
+[[Category: Holz, R C.]]
 [[Category: Moulin, A.]]
 [[Category: Munih, P.]]
-[[Category: Petsko, G.A.]]
+[[Category: Petsko, G A.]]
 [[Category: Ringe, D.]]
-[[Category: Stamper, C.C.]]
+[[Category: Stamper, C C.]]
 [[Category: CO]]
 [[Category: TRS]]
@@ Line 30: / Line 30: @@
 [[Category: x-ray]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:57:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:32:26 2008''