2prq

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[[Image:2prq.jpg|left|200px]]<br /><applet load="2prq" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2prq.jpg|left|200px]]
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caption="2prq, resolution 2.150&Aring;" />
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'''X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica'''<br />
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{{Structure
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|PDB= 2prq |SIZE=350|CAPTION= <scene name='initialview01'>2prq</scene>, resolution 2.150&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10]
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|GENE=
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}}
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'''X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2PRQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus] with <scene name='pdbligand=CO:'>CO</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRQ OCA].
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2PRQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRQ OCA].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/17574677 17574677]
[[Category: Bacterial leucyl aminopeptidase]]
[[Category: Bacterial leucyl aminopeptidase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: metalloprotease]]
[[Category: metalloprotease]]
[[Category: peptidase]]
[[Category: peptidase]]
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[[Category: tris]]
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[[Category: tri]]
[[Category: x-ray]]
[[Category: x-ray]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:32:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:16:43 2008''

Revision as of 16:16, 20 March 2008

Image:2prq.jpg


PDB ID 2prq

Drag the structure with the mouse to rotate
, resolution 2.150Å
Ligands: and
Activity: Bacterial leucyl aminopeptidase, with EC number 3.4.11.10
Coordinates: save as pdb, mmCIF, xml



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

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