4arf: Difference between revisions
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<StructureSection load='4arf' size='340' side='right' caption='[[4arf]], [[Resolution|resolution]] 1.77Å' scene=''> | <StructureSection load='4arf' size='340' side='right' caption='[[4arf]], [[Resolution|resolution]] 1.77Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4arf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ARF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ARF FirstGlance]. <br> | <table><tr><td colspan='2'>[[4arf]] is a 2 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=4ARF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ARF 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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IP8:ISOPENTENYL+PHOSPHATE'>IP8</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IP8:ISOPENTENYL+PHOSPHATE'>IP8</scene></td></tr> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4arf" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4arf" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus histolyticus weinberg and seguin 1916]] | |||
[[Category: Microbial collagenase]] | [[Category: Microbial collagenase]] | ||
[[Category: Brandstetter, H]] | [[Category: Brandstetter, H]] | ||
Revision as of 09:33, 7 February 2018
CRYSTAL STRUCTURE OF THE PEPTIDASE DOMAIN OF COLLAGENASE H FROM CLOSTRIDIUM HISTOLYTICUM IN COMPLEX WITH THE PEPTIDIC INHIBITOR ISOAMYLPHOSPHONYL-GLY-PRO-ALA AT 1.77 ANGSTROM RESOLUTION.CRYSTAL STRUCTURE OF THE PEPTIDASE DOMAIN OF COLLAGENASE H FROM CLOSTRIDIUM HISTOLYTICUM IN COMPLEX WITH THE PEPTIDIC INHIBITOR ISOAMYLPHOSPHONYL-GLY-PRO-ALA AT 1.77 ANGSTROM RESOLUTION.
Structural highlights
Publication Abstract from PubMedClostridial 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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