5boe
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Crystal structure of Staphylococcus aureus enolase in complex with PEP== |
- | + | <StructureSection load='5boe' size='340' side='right' caption='[[5boe]], [[Resolution|resolution]] 1.60Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5boe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BOE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BOE FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEP:PHOSPHOENOLPYRUVATE'>PEP</scene></td></tr> | |
- | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bof|5bof]]</td></tr> | |
- | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </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=5boe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5boe OCA], [http://pdbe.org/5boe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5boe RCSB], [http://www.ebi.ac.uk/pdbsum/5boe PDBsum]</span></td></tr> |
- | [[ | + | </table> |
- | [ | + | == Function == |
- | [[ | + | [[http://www.uniprot.org/uniprot/ENO_STAAU ENO_STAAU]] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity). Binds laminin when expressed on the bacterial cell surface; this probably induces destruction of the extracellular matrix, favoring invasion and dissemination.[HAMAP-Rule:MF_00318]<ref>PMID:15158195</ref> |
- | [[ | + | == References == |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Phosphopyruvate hydratase]] | ||
[[Category: Han, L]] | [[Category: Han, L]] | ||
+ | [[Category: Wang, C L]] | ||
+ | [[Category: Wu, M H]] | ||
+ | [[Category: Wu, Y F]] | ||
+ | [[Category: Zang, J Y]] | ||
+ | [[Category: Zhang, X]] | ||
+ | [[Category: Enolase]] | ||
+ | [[Category: Lyase]] | ||
+ | [[Category: Pep]] |
Revision as of 13:48, 9 December 2015
Crystal structure of Staphylococcus aureus enolase in complex with PEP
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