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4on1

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==Crystal Structure of metalloproteinase-II from Bacteroides fragilis==
==Crystal Structure of metalloproteinase-II from Bacteroides fragilis==
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<StructureSection load='4on1' size='340' side='right' caption='[[4on1]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
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<StructureSection load='4on1' size='340' side='right'caption='[[4on1]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4on1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacteroides_inaequalis"_eggerth_and_gagnon_1933 "bacteroides inaequalis" eggerth and gagnon 1933]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ON1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ON1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4on1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_fragilis Bacteroides fragilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ON1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ON1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.13&#8491;</td></tr>
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<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=4on1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4on1 OCA], [http://pdbe.org/4on1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4on1 RCSB], [http://www.ebi.ac.uk/pdbsum/4on1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4on1 ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4on1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4on1 OCA], [https://pdbe.org/4on1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4on1 RCSB], [https://www.ebi.ac.uk/pdbsum/4on1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4on1 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/O68424_BACFG O68424_BACFG]
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Bacteroides fragilis causes the majority of anaerobic infections in humans. The presence of a pathogenicity island in the genome discriminates pathogenic and commensal B. fragilis strains. The island encodes metalloproteinase II (MPII), a potential virulence protein, and one of three homologous fragilysin isozymes (FRA; also termed B. fragilis toxin or BFT). Here, we report biochemical data on the structural-functional characteristics of the B. fragilis pathogenicity island proteases by reporting the crystal structure of MPII at 2.13 A resolution, combined with detailed characterization of the cleavage preferences of MPII and FRA3 (as a representative of the FRA isoforms), identified using a high-throughput peptide cleavage assay with 18 583 substrate peptides. We suggest that the evolution of the MPII catalytic domain can be traced to human and archaebacterial proteinases, whereas the prodomain fold is a feature specific to MPII and FRA. We conclude that the catalytic domain of both MPII and FRA3 evolved differently relative to the prodomain, and that the prodomain evolved specifically to fit the B. fragilis pathogenicity. Overall, our data provide insights into the evolution of cleavage specificity and activation mechanisms in the virulent metalloproteinases.
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Structural and functional diversity of metalloproteinases encoded by the Bacteroides fragilis pathogenicity island.,Shiryaev SA, Aleshin AE, Muranaka N, Kukreja M, Routenberg DA, Remacle AG, Liddington RC, Cieplak P, Kozlov IA, Strongin AY FEBS J. 2014 Jun;281(11):2487-502. doi: 10.1111/febs.12804. Epub 2014 Apr 22. PMID:24698179<ref>PMID:24698179</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4on1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacteroides inaequalis eggerth and gagnon 1933]]
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[[Category: Bacteroides fragilis]]
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[[Category: Aleshin, A E]]
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[[Category: Large Structures]]
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[[Category: Liddington, R C]]
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[[Category: Aleshin AE]]
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[[Category: Shiryaev, S A]]
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[[Category: Liddington RC]]
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[[Category: Strongin, A Y]]
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[[Category: Shiryaev SA]]
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[[Category: Extracellular]]
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[[Category: Strongin AY]]
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[[Category: Fragilysin]]
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[[Category: Human pathogen]]
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[[Category: Hydrolase]]
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[[Category: Metalloproteinase]]
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[[Category: Pathogenicity island]]
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Current revision

Crystal Structure of metalloproteinase-II from Bacteroides fragilis

PDB ID 4on1

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