4d0y

Crystal structure of DacB from Streptococcus pneumoniae D39

spinqualitylabelsall models 4d0y, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d0y is a 2 chain structure with sequence from Streptococcus pneumoniae D39. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: PO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2ZP28_STRP2 Publication Abstract from PubMed Bacterial cell wall hydrolases are essential for peptidoglycan turnover and crucial to preserve cell shape. The d,d-carboxypeptidase DacA and l,d-carboxypeptidase DacB of Streptococcus pneumoniae function in a sequential manner. Here, we determined the structure of the surface-exposed lipoprotein DacB. The crystal structure of DacB, radically different to that of DacA, contains a mononuclear Zn2+ catalytic center located in the middle of a large and fully exposed groove. Two different conformations were found presenting a different arrangement of the active site topology. The critical residues for catalysis and substrate specificity were identified. Loss-of-function of DacA and DacB altered the cell shape and this was consistent with a modified peptidoglycan peptide composition in dac-mutants. Contrary, an lgt-mutant lacking lipoprotein diacylglyceryl transferase activity required for proper lipoprotein maturation retained l,d-carboxypeptidase activity and showed an intact murein sacculus. In addition we demonstrated pathophysiological effects of disabled DacA or DacB activities. Real-time bioimaging of intranasal infected mice indicated a substantial attenuation of DeltadacB and DeltadacADeltadacB pneumococci, while DeltadacA had no significant effect. In addition, uptake of these mutants by professional phagocytes was enhanced, while the adherence to lung epithelial cells was decreased. Thus, structural and functional studies suggest DacA and DacB as optimal drug targets. Structure of the pneumococcal l,d-carboxypeptidase DacB and pathophysiological effects of disabled cell wall hydrolases DacA and DacB.,Abdullah MR, Gutierrez-Fernandez J, Pribyl T, Gisch N, Saleh M, Rohde M, Petruschka L, Burchhardt G, Schwudke D, Hermoso JA, Hammerschmidt S Mol Microbiol. 2014 Jul 24. doi: 10.1111/mmi.12729. PMID:25060741 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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