1f1s: Difference between revisions

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 <StructureSection load='1f1s' size='340' side='right'caption='[[1f1s]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[1f1s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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'>[https://proteopedia.org/fgij/fg.htm?mol=1f1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1s OCA], [https://pdbe.org/1f1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f1s RCSB], [https://www.ebi.ac.uk/pdbsum/1f1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f1s ProSAT]</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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f1s ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/HYSA_STRA3 HYSA_STRA3]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f1s ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Streptococcus 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<ref>PMID:11527972</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1f1s" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Hyaluronidase 3D structures|Hyaluronidase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Streptoccocus de la mammite nocard and mollereau 1887]]
-[[Category: Hyaluronate lyase]]
 [[Category: Large Structures]]
-[[Category: Jedrzejas, M J]]
+[[Category: Streptococcus agalactiae]]
-[[Category: Li, S]]
+[[Category: Jedrzejas MJ]]
-[[Category: Lyase]]
+[[Category: Li S]]
-[[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]]