7zoc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 7zoc is ON HOLD until Paper Publication
+
==Crystal structure of the peptidase domain of collagenase H from Clostridium histolyticum in complex with N-aryl-2-alkylmercaptoacetamide-based inhibitor==
-
 
+
<StructureSection load='7zoc' size='340' side='right'caption='[[7zoc]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
-
Authors:
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[7zoc]] 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=7ZOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZOC FirstGlance]. <br>
-
Description:
+
</td></tr><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=T8E:~{N}-(4-ethanoylphenyl)-2-sulfanyl-propanamide'>T8E</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
[[Category: Unreleased Structures]]
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7zoc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zoc OCA], [https://pdbe.org/7zoc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zoc RCSB], [https://www.ebi.ac.uk/pdbsum/7zoc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zoc ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[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>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Hathewaya histolytica]]
 +
[[Category: Large Structures]]
 +
[[Category: Brandstetter H]]
 +
[[Category: Schoenauer E]]

Revision as of 06:49, 10 May 2023

Crystal structure of the peptidase domain of collagenase H from Clostridium histolyticum in complex with N-aryl-2-alkylmercaptoacetamide-based inhibitor

PDB ID 7zoc

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7zoc"
Personal tools