4p3y | pdb_00004p3y

Crystal structure of Acinetobacter baumannii DsbA in complex with EF-Tu

spinqualitylabelsall models 4p3y, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4p3y is a 2 chain structure with sequence from Acinetobacter baumannii AYE and Escherichia coli BL21(DE3). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.154Å Ligands: GDP, GOL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B0V5X3_ACIBY Publication Abstract from PubMed The multidrug resistant bacterium Acinetobacter baumannii is a significant cause of nosocomial infection. Biofilm formation - that requires both disulfide bond forming and chaperone-usher pathways - is a major virulence trait in this bacterium. Our biochemical characterizations show that the periplasmic A. baumannii DsbA (AbDsbA) enzyme has an oxidizing redox potential and dithiol oxidase activity. We found an unexpected non-covalent interaction between AbDsbA and the highly conserved prokaryotic elongation factor, EF-Tu. EF-Tu is a cytoplasmic protein but has been localized extracellularly in many bacterial pathogens. The crystal structure of this complex revealed that the EF-Tu switch I region binds to the non-catalytic surface of AbDsbA. Though the physiological and pathological significance of a DsbA/EF-Tu association is unknown, peptides derived from the EF-Tu switch I region bound to AbDsbA with submicromolar affinity. We also identified a 7-residue DsbB-derived peptide that bound to AbDsbA with low micromolar affinity. Further characterization confirmed that the EF-Tu and DsbB derived peptides bind at two distinct sites. These data point to the possibility that the non-catalytic surface of DsbA is a potential substrate or regulatory protein interaction site. The two peptides identified in this work, together with the newly characterized interaction site, provide a novel starting point for inhibitor design targeting AbDsbA. Structure of the Acinetobacter Baumannii Dithiol Oxidase DsbA Bound to EF-Tu Reveals a Novel Protein Interaction Site.,Premkumar L, Kurth F, Duprez W, Groftehauge MK, King GJ, Halili MA, Heras B, Martin JL J Biol Chem. 2014 May 23. pii: jbc.M114.571737. PMID:24860094 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures

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