Journal:Acta Cryst F:S2053230X24012056

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<b>Molecular Tour</b><br>
<b>Molecular Tour</b><br>
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''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_png/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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<b>References</b><br>
<b>References</b><br>

Revision as of 20:05, 16 January 2025

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.

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Joel L. Sussman, Jaime Prilusky

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