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| | <StructureSection load='3fh4' size='340' side='right'caption='[[3fh4]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='3fh4' size='340' side='right'caption='[[3fh4]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3fh4]] 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=3FH4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3FH4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3fh4]] 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=3FH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FH4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2iq6|2iq6]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3fh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fh4 OCA], [https://pdbe.org/3fh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fh4 RCSB], [https://www.ebi.ac.uk/pdbsum/3fh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fh4 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3fh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fh4 OCA], [http://pdbe.org/3fh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fh4 RCSB], [http://www.ebi.ac.uk/pdbsum/3fh4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fh4 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: Bennett, B]] | + | [[Category: Vibrio proteolyticus]] |
| - | [[Category: Hartley, M]] | + | [[Category: Bennett B]] |
| - | [[Category: Kim, J J.P]] | + | [[Category: Hartley M]] |
| - | [[Category: Yong, W]] | + | [[Category: Kim J-JP]] |
| - | [[Category: Aminopeptidase]]
| + | [[Category: Yong W]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Recombinant vibrio proteolyticus aminopeptidase]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Zinc]]
| + | |
| - | [[Category: Zymogen]]
| + | |
| 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
Metalloaminopeptidases (mAPs) are enzymes that are involved in HIV infectivity, tumor growth and metastasis, angiogenesis, and bacterial infection. Investigation of structure-function relationships in mAPs is a prerequisite to rational design of anti-mAP chemotherapeutics. The most intensively studied member of the biomedically important dinuclear mAPs is the prototypical secreted Vibrio proteolyticus di-zinc aminopeptidase (VpAP). The wild-type enzyme is readily purified from the supernatant of cultures of V. proteolyticus, but recombinant variants require expression in Escherichia coli. A greatly improved system for the purification of recombinant VpAP is described. A VpAP-(His)(6) polypeptide, containing an N-terminal propeptide, and a C-terminal (His)(6) adduct, was purified by metal ion affinity chromatography from the supernatant of cultures of E. coli. This single step replaced the sequence of (NH(4))(2)SO(4) fractionation, and anion-exchange and hydrophobic interaction chromatographic separations of earlier methods. Traditionally, recombinant VpAP proenzyme has been treated with proteinase K and with heat (70 degrees C), to remove the N- and C-terminal regions, and yield the mature active enzyme. This method is unsuitable for VpAP variants that are unstable towards these treatments. In the new method, the hitherto noted, but not fully appreciated, ability of VpAP to autocatalyze the hydrolysis of the N-terminal propeptide and C-terminal regions was exploited; extensive dialysis of the highly purified VpAP-(His)(6) full-length polypeptide yielded the mature active protein without recourse to proteinase K or heat treatment. Purification of variants that have previously defied isolation as mature forms of the protein was thus carried out.
Heterologous expression and purification of Vibrio proteolyticus (Aeromonas proteolytica) aminopeptidase: a rapid protocol.,Hartley M, Yong W, Bennett B Protein Expr Purif. 2009 Jul;66(1):91-101. Epub 2009 Feb 20. PMID:19233285[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hartley M, Yong W, Bennett B. Heterologous expression and purification of Vibrio proteolyticus (Aeromonas proteolytica) aminopeptidase: a rapid protocol. Protein Expr Purif. 2009 Jul;66(1):91-101. Epub 2009 Feb 20. PMID:19233285 doi:10.1016/j.pep.2009.02.011
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