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9cme

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Current revision (08:29, 14 January 2026) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9cme is ON HOLD until Paper Publication
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==Room Temperature Crystal Structure of Collagenase ColH from Hathewaya histolytica at 2.7 Angstrom resolution==
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<StructureSection load='9cme' size='340' side='right'caption='[[9cme]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9cme]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hathewaya_histolytica Hathewaya histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CME FirstGlance]. <br>
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Description:
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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]] 2.7&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=9cme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cme OCA], [https://pdbe.org/9cme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cme RCSB], [https://www.ebi.ac.uk/pdbsum/9cme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cme ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/COLH_HATHI COLH_HATHI] Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (PubMed:3002446). The full-length protein has collagenase activity, while both the 116 kDa and 98 kDa forms act on gelatin (PubMed:7961400). In vitro digestion of soluble calf skin collagen fibrils requires both ColG and ColH; ColG forms missing the second collagen-binding domain is also synergistic with ColH, although their overall efficiency is decreased (PubMed:18374061, PubMed:22099748). Digestion of collagen requires Ca(2+) and is inhibited by EDTA (PubMed:9452493). The activator domain (residues 119-388) and catalytic subdomain (330-601) open and close around substrate allowing digestion when the protein is closed (PubMed:23703618).<ref>PMID:18374061</ref> <ref>PMID:18937627</ref> <ref>PMID:22099748</ref> <ref>PMID:23703618</ref> <ref>PMID:24125730</ref> <ref>PMID:28820255</ref> <ref>PMID:3002446</ref> <ref>PMID:7961400</ref> <ref>PMID:9452493</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: Hathewaya histolytica]]
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[[Category: Large Structures]]
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[[Category: Bonsu A]]
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[[Category: Kawahara K]]
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[[Category: Matsushita O]]
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[[Category: Mima T]]
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[[Category: Oki H]]
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[[Category: Sakon J]]
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[[Category: Takebe K]]

Current revision

Room Temperature Crystal Structure of Collagenase ColH from Hathewaya histolytica at 2.7 Angstrom resolution

PDB ID 9cme

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