3ufa

Crystal structure of the staphylococcal serine protease SplA in complex with a specific phosphonate inhibitor

spinqualitylabelsall models 3ufa, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ufa is a 2 chain structure with sequence from Staphylococcus aureus subsp. aureus NCTC 8325. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: CL, VPF Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SPLA_STAA8 Publication Abstract from PubMed Staphylococcus aureus is responsible for a variety of human infections, including life-threatening, systemic conditions. Secreted proteome, including a range of proteases, constitutes the major virulence factor of the bacterium. However, the functions of individual enzymes, in particular SplA protease, remain poorly characterized. Here, we report development of specific inhibitors of SplA protease. The design, synthesis, and activity of a series of alpha-aminoalkylphosphonate diaryl esters and their peptidyl derivatives are described. Potent inhibitors of SplA are reported, which may facilitate future investigation of physiological function of the protease. The binding modes of the high-affinity compounds Cbz-PheP -(OC6 H4 -4-SO2 CH3 )2 and Suc-Val-Pro-PheP -(OC6 H5 )2 are revealed by high-resolution crystal structures of complexes with the protease. Surprisingly, the binding mode of both compounds deviates from previously characterized canonical interaction of alpha-aminoalkylphosphonate peptidyl derivatives and family S1 serine proteases. Development and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureus.,Burchacka E, Zdzalik M, Niemczyk JS, Pustelny K, Popowicz G, Wladyka B, Dubin A, Potempa J, Sienczyk M, Dubin G, Oleksyszyn J Protein Sci. 2013 Dec 4. doi: 10.1002/pro.2403. PMID:24375505 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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