Journal:Acta Cryst F:S2053230X24012056
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
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 less than 35% sequence identity to any reported structure in the protein data bank. A biotinyl-5-ATP molecule sits in a well-conserved cavity. HpBPL shares extensive tertiary structural similarity 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. | 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 less than 35% sequence identity to any reported structure in the protein data bank. A biotinyl-5-ATP molecule sits in a well-conserved cavity. HpBPL shares extensive tertiary structural similarity 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. | ||
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<b>References</b><br> | <b>References</b><br> | ||
<references/> | <references/> | ||
</StructureSection> | </StructureSection> | ||
__NOEDITSECTION__ | __NOEDITSECTION__ | ||
Revision as of 08:32, 12 December 2024
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
