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[[Image:2prq.jpg|left|200px]]<br /><applet load="2prq" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2prq, resolution 2.150&Aring;" />
'''X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica'''<br />


==Overview==
==X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica==
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.
<StructureSection load='2prq' size='340' side='right'caption='[[2prq]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2prq]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PRQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2prq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2prq OCA], [https://pdbe.org/2prq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2prq RCSB], [https://www.ebi.ac.uk/pdbsum/2prq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2prq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMPX_VIBPR AMPX_VIBPR]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/2prq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2prq ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:17574677</ref>
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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
[[Category: Bacterial leucyl aminopeptidase]]
<div class="pdbe-citations 2prq" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
 
==See Also==
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio proteolyticus]]
[[Category: Vibrio proteolyticus]]
[[Category: Bennet, B.]]
[[Category: Bennet B]]
[[Category: Holz, R.C.]]
[[Category: Holz RC]]
[[Category: Moulin, A.]]
[[Category: Moulin A]]
[[Category: Munih, P.]]
[[Category: Munih P]]
[[Category: Petsko, G.A.]]
[[Category: Petsko GA]]
[[Category: Ringe, D.]]
[[Category: Ringe D]]
[[Category: Stamper, C.C.]]
[[Category: Stamper CC]]
[[Category: CO]]
[[Category: TRS]]
[[Category: aminohydrolase]]
[[Category: cobalt]]
[[Category: metalloprotease]]
[[Category: peptidase]]
[[Category: tris]]
[[Category: x-ray]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:57:23 2008''

Latest revision as of 14:07, 30 August 2023

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

Structural highlights

2prq is a 1 chain structure with sequence from Vibrio proteolyticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMPX_VIBPR

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Munih P, Moulin A, Stamper CC, Bennett B, Ringe D, Petsko GA, Holz RC. X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica. J Inorg Biochem. 2007 Aug;101(8):1099-107. Epub 2007 Apr 11. PMID:17574677 doi:10.1016/j.jinorgbio.2007.03.010

2prq, resolution 2.15Å

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