5boe

Crystal structure of Staphylococcus aureus enolase in complex with PEP

spinqualitylabelsall models 5boe, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5boe is a 2 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: GOL, MG, PEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Enolase 3D structures

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