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'''Unreleased structure'''
==Crystal structure of Staphylococcus aureus enolase in complex with PEP==
 
<StructureSection load='5boe' size='340' side='right' caption='[[5boe]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
The entry 5boe is ON HOLD  until Paper Publication
== 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>
Authors: Wang, C.L., Wu, Y.F., Han, L., Wu, M.H., Zhang, X., Zang, J.Y.
</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>
Description: Crystal structure of Staphylococcus aureus enolase in complex with PEP
<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>
[[Category: Unreleased Structures]]
<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>
[[Category: Wang, C.L]]
</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 ==
<references/>
__TOC__
</StructureSection>
[[Category: Phosphopyruvate hydratase]]
[[Category: Han, L]]
[[Category: Wang, C L]]
[[Category: Wu, M H]]
[[Category: Wu, Y F]]
[[Category: Zang, J Y]]
[[Category: Zhang, X]]
[[Category: Zhang, X]]
[[Category: Zang, J.Y]]
[[Category: Enolase]]
[[Category: Wu, Y.F]]
[[Category: Lyase]]
[[Category: Wu, M.H]]
[[Category: Pep]]
[[Category: Han, L]]

Revision as of 16:48, 9 December 2015

Crystal structure of Staphylococcus aureus enolase in complex with PEPCrystal structure of Staphylococcus aureus enolase in complex with PEP

Structural highlights

5boe is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:Phosphopyruvate hydratase, with EC number 4.2.1.11
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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][1]

References

  1. ↑ Carneiro CR, Postol E, Nomizo R, Reis LF, Brentani RR. Identification of enolase as a laminin-binding protein on the surface of Staphylococcus aureus. Microbes Infect. 2004 May;6(6):604-8. PMID:15158195 doi:http://dx.doi.org/10.1016/j.micinf.2004.02.003

5boe, resolution 1.60Å

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