1egu
From Proteopedia
(Difference between revisions)
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<StructureSection load='1egu' size='340' side='right'caption='[[1egu]], [[Resolution|resolution]] 1.56Å' scene=''> | <StructureSection load='1egu' size='340' side='right'caption='[[1egu]], [[Resolution|resolution]] 1.56Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1egu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1egu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGU FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1egu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egu OCA], [https://pdbe.org/1egu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egu RCSB], [https://www.ebi.ac.uk/pdbsum/1egu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egu ProSAT]</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=1egu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egu OCA], [https://pdbe.org/1egu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egu RCSB], [https://www.ebi.ac.uk/pdbsum/1egu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HYSA_STRPN HYSA_STRPN] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[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=1egu ConSurf]. | </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=1egu ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Streptococcus pneumoniae hyaluronate lyase (spnHL) is a pathogenic bacterial spreading factor and cleaves hyaluronan, an important constituent of the extra- cellular matrix of connective tissues, through an enzymatic beta-elimination process, different from the hyaluronan degradation by hydrolases in animals. The mechanism of hyaluronan binding and degradation was proposed based on the 1.56 A resolution crystal structure, substrate modeling and mutagenesis studies on spnHL. Five mutants, R243V, N349A, H399A, Y408F and N580G, were constructed and their activities confirmed our mechanism hypothesis. The important roles of Tyr408, Asn349 and His399 in enzyme catalysis were proposed, explained and confirmed by mutant studies. The remaining weak enzymatic activity of the H399A mutant, the role of the free carboxylate group on the glucuronate residue, the enzymatic behavior on chondroitin and chondroitin sulfate, and the small activity increase in the N580G mutant were explained based on this mechanism. A possible function of the C-terminal beta-sheet domain is to modulate enzyme activity through binding to calcium ions. | ||
| - | |||
| - | Structural basis of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase.,Li S, Kelly SJ, Lamani E, Ferraroni M, Jedrzejas MJ EMBO J. 2000 Mar 15;19(6):1228-40. PMID:10716923<ref>PMID:10716923</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1egu" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Hyaluronidase 3D structures|Hyaluronidase 3D structures]] | *[[Hyaluronidase 3D structures|Hyaluronidase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Hyaluronate lyase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Ferraroni | + | [[Category: Streptococcus pneumoniae]] |
| - | [[Category: Jedrzejas | + | [[Category: Ferraroni M]] |
| - | [[Category: Kelly | + | [[Category: Jedrzejas MJ]] |
| - | [[Category: Lamani | + | [[Category: Kelly SJ]] |
| - | [[Category: Li | + | [[Category: Lamani E]] |
| - | + | [[Category: Li S]] | |
Current revision
CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE AT 1.56 A RESOLUTION
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