3zlg

Structure of group A Streptococcal enolase K362A mutant

spinqualitylabelsall models 3zlg, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zlg is a 4 chain structure with sequence from Streptococcus pyogenes MGAS10394. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ENO_STRP6 Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. Binds plasminogen when expressed on the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to tissue invasion and virulence. Publication Abstract from PubMed Group A Streptococcus (GAS) is a human pathogen that has the potential to cause invasive disease by binding and activating human plasmin(ogen). Streptococcal surface enolase (SEN) is an octameric alpha-enolase that is localized at the GAS cell surface. In addition to its glycolytic role inside the cell, SEN functions as a receptor for plasmin(ogen) on the bacterial surface, but the understanding of the molecular basis of plasmin(ogen) binding is limited. In this study, we determined the crystal and solution structures of GAS SEN and characterized the increased plasminogen binding by two SEN mutants. The plasminogen binding ability of SENK312A and SENK362A is ~2- and ~3.4-fold greater than for the wild-type protein. A combination of thermal stability assays, native mass spectrometry and X-ray crystallography approaches shows that increased plasminogen binding ability correlates with decreased stability of the octamer. We propose that decreased stability of the octameric structure facilitates the access of plasmin(ogen) to its binding sites, leading to more efficient plasmin(ogen) binding and activation. Stability of the octameric structure affects plasminogen-binding capacity of streptococcal enolase.,Cork AJ, Ericsson DJ, Law RH, Casey LW, Valkov E, Bertozzi C, Stamp A, Jovcevski B, Aquilina JA, Whisstock JC, Walker MJ, Kobe B PLoS One. 2015 Mar 25;10(3):e0121764. doi: 10.1371/journal.pone.0121764., eCollection 2015. PMID:25807546 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Enolase 3D structures

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