6r5b

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m (Protected "6r5b" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6r5b is ON HOLD
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==Crystal structure of PPEP-1(W103H/E143A/Y178F) in complex with substrate peptide Ac-EVNPPVP-CONH2==
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<StructureSection load='6r5b' size='340' side='right'caption='[[6r5b]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
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Authors: Pichlo, C., Wojtalla, F., Baumann, U.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6r5b]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R5B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R5B FirstGlance]. <br>
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Description: Crystal structure of PPEP-1(W103H/E143A/Y178F) in complex with substrate peptide Ac-EVNPPVP-CONH2
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=LPD:L-PROLINAMIDE'>LPD</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pro-Pro_endopeptidase Pro-Pro endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.89 3.4.24.89] </span></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=6r5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r5b OCA], [http://pdbe.org/6r5b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r5b RCSB], [http://www.ebi.ac.uk/pdbsum/6r5b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r5b ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/PPEP1_PEPD6 PPEP1_PEPD6]] Zinc-dependent endoprotease with a unique preference for proline residues surrounding the scissile bond. Exhibits a high preference for an asparagine at the P2 position and hydrophobic residues (Val, Ile, Leu) at the P3 position. Efficiently cleaves the LPXTG cell surface proteins CD630_28310 and CD630_32460 at multiple cleavage sites in vivo. Has a role in the regulation of C.difficile adhesion versus motility by cleaving surface adhesion proteins such as the collagen binding protein CD630_28310, and is important for efficient infection. Is also able to cleave fibronectin and fibrinogen in vitro; cleaves at the N-terminus of the beta-chain of fibrinogen. Destabilizes the fibronectin network produced by human fibroblasts. Therefore, may be important in key steps of clostridial pathogenesis by degrading extracellular matrix components associated with the gut epithelial cells. To a lesser extent, IgA1, IgA2, and human HSP 90-beta, but not HSP 90-alpha, are also substrates for the enzyme. Is not active on different collagen types, casein and gelatin.<ref>PMID:24303041</ref> <ref>PMID:24623589</ref> <ref>PMID:26283789</ref> <ref>PMID:26522134</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pro-Pro endopeptidase]]
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[[Category: Baumann, U]]
[[Category: Pichlo, C]]
[[Category: Pichlo, C]]
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[[Category: Baumann, U]]
 
[[Category: Wojtalla, F]]
[[Category: Wojtalla, F]]
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[[Category: Clostridium difficile]]
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[[Category: Hydrolase]]
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[[Category: Pro-pro endopeptidase 1]]
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[[Category: Virulence factor]]
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[[Category: Zinc metallopeptidase]]

Revision as of 05:50, 12 June 2019

Crystal structure of PPEP-1(W103H/E143A/Y178F) in complex with substrate peptide Ac-EVNPPVP-CONH2

PDB ID 6r5b

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