Journal:Acta Cryst F:S2053230X24012056
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| - | + | <StructureSection load='' size='450' side='right' caption='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]])' scene='10/1067687/012_starting_scene__6ck0/1'> | |
| - | <StructureSection load=' | + | ===Co-crystal structure of ''Helicobacter pylori'' biotin acetyl-CoA carboxylase synthetase (biotin protein ligase) with biotinyl-5-ATP=== |
| - | + | <big>Jesuferanmi P. Ayanlade, Dylan E. Davis, Sandhya Subramanian, David Dranow, Donald D. Lorimer, Brad Hammerson, Peter J. Myler, and Oluwatoyin A. Asojo</big> <ref>doi: 10.1107/S2053230X24012056</ref> | |
| - | + | <hr/> | |
| - | + | <b>Molecular Tour</b><br> | |
| - | + | ''Helicobacter pylori'', a type 1 carcinogen that causes human gastric ulcers and cancer, is a priority target of the [http://www.ssgcid.org 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 <scene name='10/1067687/3b/1'>less than 35% sequence identity to any reported structure</scene> in the [http://www.rcsb.org Protein Data Bank] via analysis with ENDScript<ref>PMID:12824317</ref><ref>PMID:24753421</ref>. It crystalizes as a <scene name='10/1067687/2a/1'>dimer</scene>. A biotinyl-5-ATP molecule sits in a <scene name='10/1067687/3a/1'>well-conserved cavity</scene>. HpBPL shares <scene name='10/1067687/3c/1'>extensive tertiary structural similarity</scene> 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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| + | '''References''' | ||
<references/> | <references/> | ||
</StructureSection> | </StructureSection> | ||
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