Journal:Acta Cryst F:S2053230X24012056
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| - | <StructureSection load='' size='450' side='right' scene='10/1067687/012_fig_3c_pngj/ | + | <StructureSection load='' size='450' side='right' scene='10/1067687/012_fig_3c_pngj/2' caption='H. pylori biotin protein ligase is shown as a cartoon, colored in a rainbow from blue N-ter to red C-ter. Biotin is shown as balls and sticks.'> |
===Co-crystal structure of ''Helicobacter pylori'' biotin acetyl-CoA carboxylase synthetase (biotin protein ligase) with biotinyl-5-ATP=== | ===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> | <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/> | <hr/> | ||
<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 [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='10/1067687/012_fig_3b_png/2'>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='10/1067687/012_fig_2a_new_png/4'>dimer</scene>. A biotinyl-5-ATP molecule sits in a <scene name='10/1067687/012_fig_3a_png/1'>well-conserved cavity</scene>. HpBPL shares <scene name='10/1067687/012_fig_3c_pngj/ | + | ''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='10/1067687/012_fig_3b_png/2'>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='10/1067687/012_fig_2a_new_png/4'>dimer</scene>. A biotinyl-5-ATP molecule sits in a <scene name='10/1067687/012_fig_3a_png/1'>well-conserved cavity</scene>. HpBPL shares <scene name='10/1067687/012_fig_3c_pngj/2'>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. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 20:25, 15 January 2025
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