2y3u
From Proteopedia
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| - | [[Image:2y3u.png|left|200px]] | ||
| - | + | ==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=''> | ||
| + | == Structural highlights == | ||
| + | <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='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='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='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> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:21947205</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2y3u" style="background-color:#fffaf0;"></div> | |
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==See Also== | ==See Also== | ||
| - | *[[Collagenase | + | *[[Collagenase 3D structures|Collagenase 3D structures]] |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | < | + | </StructureSection> |
| - | [[Category: | + | [[Category: Hathewaya histolytica]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Brandstetter | + | [[Category: Brandstetter H]] |
| - | [[Category: Eckhard | + | [[Category: Eckhard U]] |
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Current revision
Crystal structure of apo collagenase G from Clostridium histolyticum at 2.55 Angstrom resolution
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