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| | <StructureSection load='2prq' size='340' side='right'caption='[[2prq]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='2prq' size='340' side='right'caption='[[2prq]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2prq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aeromonas_proteolytica"_merkel_et_al._1964 "aeromonas proteolytica" merkel et al. 1964]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PRQ FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1amp|1amp]], [[1lok|1lok]]</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2prq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2prq OCA], [http://pdbe.org/2prq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2prq RCSB], [http://www.ebi.ac.uk/pdbsum/2prq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2prq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AMPX_VIBPR AMPX_VIBPR] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aeromonas proteolytica merkel et al. 1964]] | |
| - | [[Category: Bacterial leucyl aminopeptidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bennet, B]] | + | [[Category: Vibrio proteolyticus]] |
| - | [[Category: Holz, R C]] | + | [[Category: Bennet B]] |
| - | [[Category: Moulin, A]] | + | [[Category: Holz RC]] |
| - | [[Category: Munih, P]] | + | [[Category: Moulin A]] |
| - | [[Category: Petsko, G A]] | + | [[Category: Munih P]] |
| - | [[Category: Ringe, D]] | + | [[Category: Petsko GA]] |
| - | [[Category: Stamper, C C]] | + | [[Category: Ringe D]] |
| - | [[Category: Aminohydrolase]]
| + | [[Category: Stamper CC]] |
| - | [[Category: Cobalt]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metalloprotease]]
| + | |
| - | [[Category: Peptidase]]
| + | |
| - | [[Category: Tri]]
| + | |
| Structural highlights
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
- ↑ 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
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