Sandbox I3DC 012

Co-crystal structure of Helicobacter pylori biotin acetyl-CoA carboxylase synthetase (biotin protein ligase) with biotinyl-5-ATP Jesuferanmi P. Ayanlade, Dylan E. Davis, Sandhya Subramanian, David Dranow, Donald D. Lorimer, Brad Hammerson, Peter J. Myler, and Oluwatoyin A. Asojo Molecular Tour Helicobacter pylori, a type 1 carcinogen that causes human gastric ulcers and cancer, is a priority target of the Seattle Structural Genomics Center for Infectious Disease (SSGCID). These efforts include determining the structures of potential H. pylori therapeutic targets. Here, we report the purification, crystallization, and x-ray structure of one such target, H. pylori biotin protein ligase (HpBPL). HpBPL catalyzes the activation of various biotin-dependent metabolic pathways, including fatty acid synthesis, gluconeogenesis, and amino acid catabolism, and may facilitate H. pylori survival in the high pH gastric mucosa. HpBPL is a prototypical bacterial biotin protein ligase despite in the Protein Data Bank via analysis with ENDScript. It crystalizes as a . A biotinyl-5-ATP molecule sits in a . HpBPL shares to Mycobacterium tuberculosis biotin protein ligase (MtBPL), despite less than 22% sequence identity. HpBPL’s active site is very similar to MtBPL and has the necessary residues to bind inhibitors developed for MtBPL. References

spinqualitylabelsall models H. pylori biotin protein ligase is shown as a cartoon, colored in a rainbow from blue N-ter to red C-ter (PDB_ID 6ck0) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image