4wck

Crystal Structure of apo Cell Shape Determinant protein Csd4 from Helicobacter pylori

spinqualitylabelsall models 4wck, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wck is a 1 chain structure with sequence from Helicobacter pylori G27. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Ligands: API, IOD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B5ZAD9_HELPG Publication Abstract from PubMed Peptidoglycan (PG) modifying carboxypeptidases (CPs) are important determinants of bacterial cell shape. Here, we report crystal structures of Csd4, a three-domain protein from the human gastric pathogen Helicobacter pylori. The catalytic zinc in Csd4 is coordinated by a rare H+E+Q configuration that is conserved amongst most Csd4 homologs, which form a distinct subfamily of CPs. Substitution of the glutamine to histidine, the residue found in prototypical zinc carboxypeptidases, resulted in decreased enzyme activity and inhibition by phosphate. Expression of the histidine variant at the native locus in a H. pylori csd4 deletion strain did not restore the wild-type helical morphology. Biochemical assays show that Csd4 can cleave a tripeptide PG substrate analog to release m-DAP. Structures of Csd4 with this substrate analog or product bound at the active site reveal determinants of peptidoglycan specificity and the mechanism to cleave an isopeptide bond to release m-DAP. Our data suggest that Csd4 is the archetype of a new CP subfamily with a domain scheme that differs from this large family of peptide cleaving enzymes. Helical Shape of Helicobacter pylori Requires an Atypical Glutamine as a Zinc Ligand in the Carboxypeptidase Csd4.,Chan AC, Blair KM, Liu Y, Frirdich E, Gaynor EC, Tanner ME, Salama NR, Murphy ME J Biol Chem. 2014 Dec 12. pii: jbc.M114.624734. PMID:25505267 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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