2o8o: Difference between revisions

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New page: left|200px<br /><applet load="2o8o" size="350" color="white" frame="true" align="right" spinBox="true" caption="2o8o, resolution 1.35Å" /> '''Crystal structure of...
 
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[[Image:2o8o.jpg|left|200px]]<br /><applet load="2o8o" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2o8o, resolution 1.35&Aring;" />
'''Crystal structure of Clostridium histolyticum colg collagenase collagen-binding domain 3B at 1.35 Angstrom resolution in presence of calcium'''<br />


==About this Structure==
==Crystal structure of Clostridium histolyticum colg collagenase collagen-binding domain 3B at 1.35 Angstrom resolution in presence of calcium==
2O8O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_histolyticum Clostridium histolyticum] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O8O OCA].
<StructureSection load='2o8o' size='340' side='right'caption='[[2o8o]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
[[Category: Clostridium histolyticum]]
== Structural highlights ==
[[Category: Microbial collagenase]]
<table><tr><td colspan='2'>[[2o8o]] 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=2O8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O8O FirstGlance]. <br>
[[Category: Single protein]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
[[Category: Matsushita, O.]]
<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=CL:CHLORIDE+ION'>CL</scene></td></tr>
[[Category: Philominathan, S.T.L.]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o8o OCA], [https://pdbe.org/2o8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o8o RCSB], [https://www.ebi.ac.uk/pdbsum/2o8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o8o ProSAT]</span></td></tr>
[[Category: Sakon, J.]]
</table>
[[Category: Wilson, J.J]]
== Function ==
[[Category: CA]]
[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>
[[Category: CL]]
== Evolutionary Conservation ==
[[Category: helix to beta transtition]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: hydrolase]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o8/2o8o_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o8o ConSurf].
<div style="clear:both"></div>


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:43:13 2008''
==See Also==
*[[Collagenase 3D structures|Collagenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hathewaya histolytica]]
[[Category: Large Structures]]
[[Category: Matsushita O]]
[[Category: Philominathan STL]]
[[Category: Sakon J]]
[[Category: Wilson JJ]]