2rui

Solution Structure of the Bacillus anthracis Sortase A-substrate Complex

spinqualitylabelsall models 2rui Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2rui is a 2 chain structure with sequence from Bacillus anthracis str. Sterne and Synthetic construct. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: B27, BOC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q81V16_BACAN Publication Abstract from PubMed The endospore forming bacterium Bacillus anthracis causes lethal anthrax disease in humans and animals. The ability of this pathogen to replicate within macrophages is dependent upon the display of bacterial surface proteins attached to the cell wall by the B. anthracis Sortase A ((Ba)SrtA) enzyme. Previously, we discovered that the class A (Ba)SrtA sortase contains a unique N-terminal appendage that wraps around the body of the protein to contact the active site of the enzyme. To gain insight into its function, we determined the NMR structure of (Ba)SrtA bound to a LPXTG sorting signal analog. The structure, combined with dynamics, kinetics, and whole cell protein display data suggest that the N terminus modulates substrate access to the enzyme. We propose that it may increase the efficiency of protein display by reducing the unproductive hydrolytic cleavage of enzyme-protein covalent intermediates that form during the cell wall anchoring reaction. Notably, a key active site loop (beta7/beta8 loop) undergoes a disordered to ordered transition upon binding the sorting signal, potentially facilitating recognition of lipid II. Structure of the Bacillus anthracis Sortase A Enzyme Bound to Its Sorting Signal: A FLEXIBLE AMINO-TERMINAL APPENDAGE MODULATES SUBSTRATE ACCESS.,Chan AH, Yi SW, Terwilliger AL, Maresso AW, Jung ME, Clubb RT J Biol Chem. 2015 Oct 16;290(42):25461-74. doi: 10.1074/jbc.M115.670984. Epub, 2015 Aug 31. PMID:26324714 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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