NMR Structure of Acyl-Carrier Protein from Borrelia burgdorferi
Author Information
Author(s): Barnwal Ravi P., Van Voorhis Wesley C., Varani G.
Primary Institution: University of Washington
Hypothesis
The acyl-carrier protein from Borrelia burgdorferi is a potential target for drug discovery due to its role in fatty-acid biosynthesis.
Conclusion
The study successfully determined the high-resolution NMR structure of the acyl-carrier protein, revealing its potential as a target for drug development against Lyme disease.
Supporting Evidence
- The NMR structure was determined to a backbone r.m.s.d. of 0.4 Å.
- Over 98% of backbone resonances and over 92% of side-chain resonances were assigned.
- The protein is highly similar to the acyl-carrier protein from Aquifex aeolicus.
Takeaway
Scientists studied a protein from a germ that causes Lyme disease to understand how it helps the germ make fats, which could help find new medicines.
Methodology
The protein was expressed in E. coli, purified, and its structure was determined using multidimensional NMR spectroscopy.
Limitations
The study did not investigate the functional role of specific residues in catalysis through site-directed mutagenesis.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website