Structure of Helicobacter pylori Biotin Protein Ligase with Biotinyl-5-ATP
Author Information
Author(s): Ayanlade Jesuferanmi P., Davis Dylan E., Subramanian Sandhya, Dranow David M., Lorimer Donald D., Hammerson Brad, Myler Peter J., Asojo Oluwatoyin A.
Primary Institution: Dartmouth Cancer Center
Hypothesis
The study investigates the structure of Helicobacter pylori biotin protein ligase (HpBPL) to understand its potential as a drug target.
Conclusion
The study reveals a well-conserved catalytic cavity in HpBPL, suggesting that inhibitors developed for Mycobacterium tuberculosis biotin protein ligase may be repurposed for HpBPL.
Supporting Evidence
- HpBPL is essential for various metabolic pathways in Helicobacter pylori.
- The structure of HpBPL was determined at a resolution of 2.25 Å.
- HpBPL shares significant structural similarity with Mycobacterium tuberculosis biotin protein ligase.
Takeaway
Scientists looked at a protein from a germ that can cause stomach problems and found that it has a special shape that could help make new medicines.
Methodology
The protein was purified, crystallized, and its structure was determined using X-ray crystallography.
Digital Object Identifier (DOI)
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