2y72: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF THE PKD DOMAIN OF COLLAGENASE G FROM CLOSTRIDIUM HISTOLYTICUM AT 1.18 ANGSTROM RESOLUTION.==
-<StructureSection load='2y72' size='340' side='right' caption='[[2y72]], [[Resolution|resolution]] 1.18&Aring;' scene=''>
+==Crystal structure of the PKD Domain of Collagenase G from Clostridium Histolyticum at 1.18 Angstrom Resolution.==
+<StructureSection load='2y72' size='340' side='right'caption='[[2y72]], [[Resolution|resolution]] 1.18&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2y72]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_histolyticum Clostridium histolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y72 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y72 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2y72]] is a 2 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=2Y72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y72 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2y50|2y50]], [[2y3u|2y3u]], [[2y6i|2y6i]]</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]] 1.18&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Microbial_collagenase Microbial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.3 3.4.24.3] </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=2y72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y72 OCA], [https://pdbe.org/2y72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y72 RCSB], [https://www.ebi.ac.uk/pdbsum/2y72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y72 ProSAT]</span></td></tr>
-<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=2y72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y72 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y72 RCSB], [http://www.ebi.ac.uk/pdbsum/2y72 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/COLG_HATHI COLG_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). Active on soluble type I collagen, insoluble collagen, azocoll, soluble PZ-peptide (all collagenase substrates) and gelatin (PubMed:9922257). The full-length protein has collagenase activity, while the in vivo derived C-terminally truncated shorter versions only act on gelatin (PubMed:9922257). In vitro digestion of soluble calf skin collagen fibrils requires both ColG and ColH; ColG forms missing the second collagen-binding domain are also synergistic with ColH, although their overall efficiency is decreased (PubMed:18374061, PubMed:22099748). The activator domain (residues 119-388) and catalytic subdomain (389-670) open and close around substrate using a Gly-rich hinge (387-397), allowing digestion when the protein is closed (PubMed:21947205, PubMed:23703618). Binding of collagen requires Ca(2+) and is inhibited by EGTA; the collagen-binding domain (CBD, S3a plus S3b) specifically recognizes the triple-helical conformation made by 3 collagen protein chains in the triple-helical region (PubMed:11121400). Isolated CBD (S3a plus S3b) binds collagen fibrils and sheets of many tissues (PubMed:11913772).<ref>PMID:11121400</ref> <ref>PMID:11913772</ref> <ref>PMID:18374061</ref> <ref>PMID:18937627</ref> <ref>PMID:21947205</ref> <ref>PMID:22099748</ref> <ref>PMID:23703618</ref> <ref>PMID:24125730</ref> <ref>PMID:28820255</ref> <ref>PMID:3002446</ref> <ref>PMID:9922257</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 15: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2y72" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Collagenase (non-MMP)|Collagenase (non-MMP)]]
+*[[Collagenase 3D structures|Collagenase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Clostridium histolyticum]]
+[[Category: Hathewaya histolytica]]
-[[Category: Microbial collagenase]]
+[[Category: Large Structures]]
-[[Category: Brandstetter, H.]]
+[[Category: Brandstetter H]]
-[[Category: Eckhard, U.]]
+[[Category: Eckhard U]]
-[[Category: Beta barrel]]
-[[Category: Collagen recognition domain]]
-[[Category: Hydrolase]]
-[[Category: Polycystic kidney disease domain]]