4aqo
From Proteopedia
(Difference between revisions)
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| - | + | ==CRYSTAL STRUCTURE OF THE CALCIUM BOUND PKD-like DOMAIN OF COLLAGENASE G FROM CLOSTRIDIUM HISTOLYTICUM AT 0.99 ANGSTROM RESOLUTION.== | |
| - | + | <StructureSection load='4aqo' size='340' side='right' caption='[[4aqo]], [[Resolution|resolution]] 0.99Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4aqo]] is a 1 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=4AQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AQO FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2y3u|2y3u]], [[2y50|2y50]], [[2y6i|2y6i]], [[2y72|2y72]]</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=4aqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aqo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4aqo RCSB], [http://www.ebi.ac.uk/pdbsum/4aqo PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Clostridial collagenases are among the most efficient enzymes to degrade by far the most predominant protein in the biosphere. Here we present crystal structures of the peptidases of three clostridial collagenase isoforms (ColG, ColH and ColT). The comparison of unliganded and liganded structures reveal a quaternary subdomain dynamics. In the unliganded ColH structure this globular dynamics is modulated by an aspartate switch motion that binds to the catalytic zinc. We further identified a calcium binding site in proximity to the catalytic zinc. Both ions are required for full activity, explaining why calcium critically affects the enzymatic activity of clostridial collagenases. Our studies further reveal that loops close to the active site thus serve as characteristic substrate selectivity filter. These elements explain the distinct peptidolytic and collagenolytic activities of these enzymes and provide a rational to engineer collagenases with customized substrate specificity as well as for inhibitor design. | ||
| - | + | Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T.,Eckhard U, Schonauer E, Brandstetter H J Biol Chem. 2013 May 23. PMID:23703618<ref>PMID:23703618</ref> | |
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| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Clostridium histolyticum]] | [[Category: Clostridium histolyticum]] | ||
[[Category: Microbial collagenase]] | [[Category: Microbial collagenase]] | ||
| - | [[Category: Brandstetter, H | + | [[Category: Brandstetter, H]] |
| - | [[Category: Eckhard, U | + | [[Category: Eckhard, U]] |
[[Category: Collagen]] | [[Category: Collagen]] | ||
[[Category: Collagenolysis]] | [[Category: Collagenolysis]] | ||
Revision as of 09:08, 21 December 2014
CRYSTAL STRUCTURE OF THE CALCIUM BOUND PKD-like DOMAIN OF COLLAGENASE G FROM CLOSTRIDIUM HISTOLYTICUM AT 0.99 ANGSTROM RESOLUTION.
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