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| | <StructureSection load='5boe' size='340' side='right'caption='[[5boe]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='5boe' size='340' side='right'caption='[[5boe]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5boe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. 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> | + | <table><tr><td colspan='2'>[[5boe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bof|5bof]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eno ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=5boe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5boe OCA], [https://pdbe.org/5boe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5boe RCSB], [https://www.ebi.ac.uk/pdbsum/5boe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5boe ProSAT]</span></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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5boe ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [https://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphopyruvate hydratase]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Han, L]] | + | [[Category: Han L]] |
| - | [[Category: Wang, C L]] | + | [[Category: Wang CL]] |
| - | [[Category: Wu, M H]] | + | [[Category: Wu MH]] |
| - | [[Category: Wu, Y F]] | + | [[Category: Wu YF]] |
| - | [[Category: Zang, J Y]] | + | [[Category: Zang JY]] |
| - | [[Category: Zhang, X]] | + | [[Category: Zhang X]] |
| - | [[Category: Enolase]]
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| - | [[Category: Lyase]]
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| - | [[Category: Pep]]
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| Structural highlights
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]
Publication Abstract from PubMed
Staphylococcus aureus is a Gram-positive bacterium with strong pathogenicity that causes a wide range of infections and diseases. Enolase is an evolutionarily conserved enzyme that plays a key role in energy production through glycolysis. Additionally, enolase is located on the surface of S. aureus and is involved in processes leading to infection. Here, crystal structures of Sa_enolase with and without bound phosphoenolpyruvate (PEP) are presented at 1.6 and 2.45 A resolution, respectively. The structure reveals an octameric arrangement; however, both dimeric and octameric conformations were observed in solution. Furthermore, enzyme-activity assays show that only the octameric variant is catalytically active. Biochemical and structural studies indicate that the octameric form of Sa_enolase is enzymatically active in vitro and likely also in vivo, while the dimeric form is catalytically inactive and may be involved in other biological processes.
Octameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate.,Wu Y, Wang C, Lin S, Wu M, Han L, Tian C, Zhang X, Zang J Acta Crystallogr D Biol Crystallogr. 2015 Dec 1;71(Pt 12):2457-70. doi:, 10.1107/S1399004715018830. Epub 2015 Nov 26. PMID:26627653[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ Wu Y, Wang C, Lin S, Wu M, Han L, Tian C, Zhang X, Zang J. Octameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate. Acta Crystallogr D Biol Crystallogr. 2015 Dec 1;71(Pt 12):2457-70. doi:, 10.1107/S1399004715018830. Epub 2015 Nov 26. PMID:26627653 doi:http://dx.doi.org/10.1107/S1399004715018830
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