biostudies-literatureAyanlade JPNational Institute of Allergy and Infectious DiseasesNIAID NIH HHSNational Cancer InstituteNCI NIH HHS11-18https://www.ebi.ac.uk/biostudies/studies/S-EPMC11701928biostudies-literatureUnknown81(Pt 1)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, the purification, crystallization and X-ray structure of one such target, H. pylori biotin protein ligase (HpBPL), are reported. HpBPL catalyzes the activation of various biotin-dependent metabolic pathways, including fatty-acid synthesis, gluconeogenesis and amino-acid catabolism, and may facilitate the survival of H. pylori in the high-pH gastric mucosa. HpBPL is a prototypical bacterial biotin protein ligase, despite having less than 35% sequence identity to any reported structure in the Protein Data Bank. A biActa crystallographica. Section F, Structural biology communicationsCo-crystal structure of Helicobacter pylori biotin protein ligase with biotinyl-5-ATP.PMC11701928R25CA25095675N93022C00036R25 CA250956Dranow DMLorimer DDHammerson BAyanlade JPMyler PJDavis DEAsojo OASubramanian SfalseCo-crystal structure of Helicobacter pylori biotin protein ligase with biotinyl-5-ATP.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, the purification, crystallization and X-ray structure of one such target, H. pylori biotin protein ligase (HpBPL), are reported. HpBPL catalyzes the activation of various biotin-dependent metabolic pathways, including fatty-acid synthesis, gluconeogenesis and amino-acid catabolism, and may facilitate the survival of H. pylori in the high-pH gastric mucosa. HpBPL is a prototypical bacterial biotin protein ligase, despite having less than 35% sequence identity to any reported structure in the Protein Data Bank. A bi2025-01-01T00:00:00Z2025 Jan2026-06-02T18:28:46.963Z2026-04-18T03:13:45.286ZS-EPMC117019283970471910.1107/S2053230X24012056