Related Experiment Video

Updated: Jun 4, 2025

In Vitro Biochemical Assays using Biotin Labels to Study Protein-Nucleic Acid Interactions
08:14

In Vitro Biochemical Assays using Biotin Labels to Study Protein-Nucleic Acid Interactions

Published on: July 17, 2019

12.6K

Co-crystal structure of Helicobacter pylori biotin protein ligase with biotinyl-5-ATP

Jesuferanmi P Ayanlade1, Dylan E Davis1, Sandhya Subramanian2

  • 1Dartmouth Cancer Center, One Medical Center Drive, Lebanon, NH 03756, USA.

Acta Crystallographica. Section F, Structural Biology Communications
|December 20, 2024
PubMed

Insights

Helicobacter pylori biotin protein ligase (HpBPL) structure was determined. This enzyme is crucial for bacterial survival and may be a therapeutic target due to its structural similarity to Mycobacterium tuberculosis biotin protein ligase.

Area of Science:

  • Structural biology
  • Microbiology
  • Biochemistry

Background:

  • Helicobacter pylori is a carcinogen causing gastric ulcers and cancer.
  • Identifying therapeutic targets for H. pylori is a priority.
  • H. pylori biotin protein ligase (HpBPL) is essential for bacterial survival.

Purpose of the Study:

  • To determine the X-ray structure of H. pylori biotin protein ligase (HpBPL).
  • To investigate HpBPL as a potential therapeutic target.

Main Methods:

  • Purification of HpBPL.
  • Crystallization of HpBPL.
  • X-ray structure determination of HpBPL.

Main Results:

  • The X-ray structure of HpBPL was determined.
  • A biotinyl-5-ATP molecule was observed in a conserved cavity.
  • HpBPL shares structural similarity with Mycobacterium tuberculosis biotin protein ligase (MtBPL).
  • The active site of HpBPL is similar to MtBPL, suggesting potential for inhibitor binding.

Conclusions:

  • HpBPL structure provides insights into its function in H. pylori.
  • HpBPL is a potential therapeutic target, with possible cross-reactivity with MtBPL inhibitors.
Keywords:
SSGCIDcancergastric ulcersinfectious diseasesundergraduate education and training

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