1f1s: Difference between revisions
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<StructureSection load='1f1s' size='340' side='right' caption='[[1f1s]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1f1s' size='340' side='right' caption='[[1f1s]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1f1s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1f1s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptoccocus_de_la_mammite"_nocard_and_mollereau_1887 "streptoccocus de la mammite" nocard and mollereau 1887]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F1S FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i8q|1i8q]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i8q|1i8q]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hyaluronate_lyase Hyaluronate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.1 4.2.2.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hyaluronate_lyase Hyaluronate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.1 4.2.2.1] </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=1f1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f1s RCSB], [http://www.ebi.ac.uk/pdbsum/1f1s PDBsum]</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=1f1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1s OCA], [http://pdbe.org/1f1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f1s RCSB], [http://www.ebi.ac.uk/pdbsum/1f1s PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1f1s" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Streptoccocus de la mammite nocard and mollereau 1887]] | |||
[[Category: Hyaluronate lyase]] | [[Category: Hyaluronate lyase]] | ||
[[Category: Jedrzejas, M J]] | [[Category: Jedrzejas, M J]] | ||
[[Category: Li, S]] | [[Category: Li, S]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
[[Category: The structure consists of three distinct structural domains: two beta domains at two terminals and one alpha domain in the middle of the sequence]] | [[Category: The structure consists of three distinct structural domains: two beta domains at two terminals and one alpha domain in the middle of the sequence]] | ||
Revision as of 07:49, 11 September 2015
CRYSTAL STRUCTURE OF STREPTOCOCCUS AGALACTIAE HYALURONATE LYASE AT 2.1 ANGSTROM RESOLUTION.CRYSTAL STRUCTURE OF STREPTOCOCCUS AGALACTIAE HYALURONATE LYASE AT 2.1 ANGSTROM RESOLUTION.
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStreptococcus agalactiae hyaluronate lyase is a virulence factor that helps this pathogen to break through the biophysical barrier of the host tissues by the enzymatic degradation of hyaluronan and certain chondroitin sulfates at beta-1,4 glycosidic linkages. Crystal structures of the native enzyme and the enzyme-product complex were determined at 2.1- and 2.2-A resolutions, respectively. An elongated cleft transversing the middle of the molecule has been identified as the substrate-binding place. Two product molecules of hyaluronan degradation were observed bound to the cleft. The enzyme catalytic site was identified to comprise three residues: His(479), Tyr(488), and Asn(429). The highly positively charged cleft facilitates the binding of the negatively charged polymeric substrate chain. The matching between the aromatic patch of the enzyme and the hydrophobic patch of the substrate chain anchors the substrate chain into degradation position. A pair of proton exchanges between the enzyme and the substrate results in the cleavage of the beta-1,4 glycosidic linkage of the substrate chain and the unsaturation of the product. Phe(423) likely determines the size of the product at the product release side of the catalytic region. Hyaluronan chain is processively degraded from the reducing end toward the nonreducing end. The unsulfated or 6-sulfated regions of chondroitin sulfate can also be degraded in the same manner as hyaluronan. Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate lyase.,Li S, Jedrzejas MJ J Biol Chem. 2001 Nov 2;276(44):41407-16. Epub 2001 Aug 29. PMID:11527972[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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