5bof
From Proteopedia
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== 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> | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:26627653</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5bof" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 07:00, 16 December 2015
Crystal Structure of Staphylococcus aureus Enolase
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Categories: Phosphopyruvate hydratase | Han, L | Wang, C L | Wu, M H | Wu, Y F | Zang, J Y | Zhang, X | Enolase | Lyase
