Structure of Fumarate Hydratase from Rickettsia prowazekii
Author Information
Author(s): Phan Isabelle, Subramanian Sandhya, Olsen Christian, Edwards Thomas E., Guo Wenjin, Zhang Yang, Van Voorhis Wesley C., Stewart Lance J., Myler Peter J.
Primary Institution: Seattle Structural Genomics Center for Infectious Diseases
Conclusion
The structure of R. prowazekii fumarate hydratase is similar to that of human mitochondrial fumarate hydratase.
Supporting Evidence
- The structure was solved at a resolution of 2.4 Å.
- Fumarate hydratase is an enzyme involved in the tricarboxylic acid cycle.
- Rickettsia prowazekii is a causative agent of typhus.
- The study highlights the evolutionary relationship between Rickettsia and mitochondria.
- FumC from R. prowazekii crystallized as a homodimer.
- Structure alignment showed high conservation with human FumC.
- Defects in human FumC are linked to serious health conditions.
- The findings suggest that targeting FumC for drug development may not be effective.
Takeaway
Scientists studied a protein from a bacteria that causes typhus, and found it looks a lot like a similar protein in humans.
Methodology
The study involved protein expression, purification, crystallization, and structure determination using X-ray crystallography.
Limitations
The enzyme is highly conserved between R. prowazekii and humans, making it a poor target for drug development.
Digital Object Identifier (DOI)
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