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| | ==Crystal structure of apo collagenase G from Clostridium histolyticum at 2.55 Angstrom resolution== | | ==Crystal structure of apo collagenase G from Clostridium histolyticum at 2.55 Angstrom resolution== |
| - | <StructureSection load='2y3u' size='340' side='right' caption='[[2y3u]], [[Resolution|resolution]] 2.55Å' scene=''> | + | <StructureSection load='2y3u' size='340' side='right'caption='[[2y3u]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2y3u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_histolyticus"_weinberg_and_seguin_1916 "bacillus histolyticus" weinberg and seguin 1916]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y3U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2y3u]] 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=2Y3U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y3U FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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]] 2.55Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2y50|2y50]]</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=2y3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3u OCA], [https://pdbe.org/2y3u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y3u RCSB], [https://www.ebi.ac.uk/pdbsum/2y3u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3u ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3u OCA], [http://pdbe.org/2y3u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y3u RCSB], [http://www.ebi.ac.uk/pdbsum/2y3u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3u ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | ==See Also== | | ==See Also== |
| - | *[[Collagenase (non-MMP)|Collagenase (non-MMP)]] | + | *[[Collagenase 3D structures|Collagenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus histolyticus weinberg and seguin 1916]] | + | [[Category: Hathewaya histolytica]] |
| - | [[Category: Microbial collagenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Brandstetter, H]] | + | [[Category: Brandstetter H]] |
| - | [[Category: Eckhard, U]] | + | [[Category: Eckhard U]] |
| - | [[Category: Gluzincin]]
| + | |
| - | [[Category: Hydrolase]]
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| - | [[Category: Metalloprotease]]
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| Structural highlights
Publication Abstract from PubMed
Collagen constitutes one-third of body protein in humans, reflecting its extensive role in health and disease. Of similar importance, therefore, are the idiosyncratic proteases that have evolved for collagen remodeling. The most efficient collagenases are those that enable clostridial bacteria to colonize their host tissues; but despite intense study, the structural and mechanistic basis of these enzymes has remained elusive. Here we present the crystal structure of collagenase G from Clostridium histolyticum at 2.55-A resolution. By combining the structural data with enzymatic and mutagenesis studies, we derive a conformational two-state model of bacterial collagenolysis, in which recognition and unraveling of collagen microfibrils into triple helices, as well as unwinding of the triple helices, are driven by collagenase opening and closing.
Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis.,Eckhard U, Schonauer E, Nuss D, Brandstetter H Nat Struct Mol Biol. 2011 Sep 25;18(10):1109-14. doi: 10.1038/nsmb.2127. PMID:21947205[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Eckhard U, Schonauer E, Nuss D, Brandstetter H. Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis. Nat Struct Mol Biol. 2011 Sep 25;18(10):1109-14. doi: 10.1038/nsmb.2127. PMID:21947205 doi:10.1038/nsmb.2127
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