{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ayanlade JP"],"funding":["National Institute of Allergy and Infectious Diseases","NIAID NIH HHS","National Cancer Institute","NCI NIH HHS"],"pagination":["11-18"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11701928"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["81(Pt 1)"],"pubmed_abstract":["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 bi"],"journal":["Acta crystallographica. Section F, Structural biology communications"],"pubmed_title":["Co-crystal structure of Helicobacter pylori biotin protein ligase with biotinyl-5-ATP."],"pmcid":["PMC11701928"],"funding_grant_id":["R25CA250956","75N93022C00036","R25 CA250956"],"pubmed_authors":["Dranow DM","Lorimer DD","Hammerson B","Ayanlade JP","Myler PJ","Davis DE","Asojo OA","Subramanian S"],"additional_accession":[]},"is_claimable":false,"name":"Co-crystal structure of Helicobacter pylori biotin protein ligase with biotinyl-5-ATP.","description":"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 bi","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-06-02T18:28:46.963Z","creation":"2026-04-18T03:13:45.286Z"},"accession":"S-EPMC11701928","cross_references":{"pubmed":["39704719"],"doi":["10.1107/S2053230X24012056"]}}