Structure of a Nudix hydrolase from Bartonella henselae
Author Information
Author(s): Buchko Garry W., Edwards Thomas E., Abendroth Jan, Arakaki Tracy L., Law Laura, Napuli Alberto J., Hewitt Stephen N., Van Voorhis Wesley C., Stewart Lance J., Staker Bart L., Myler Peter J.
Primary Institution: Seattle Structural Genomics Center for Infectious Disease
Hypothesis
The study aims to determine the crystal structure of the Nudix hydrolase Bh-MutT in the Mg2+-bound state.
Conclusion
The crystal structure of Bh-MutT reveals its similarity to other Nudix hydrolases and highlights its functional diversity.
Supporting Evidence
- The crystal structure was determined at 2.1 Å resolution.
- The structure includes two molecules of Bh-MutT packed together in the asymmetric unit.
- The catalytically essential divalent cation Mg2+ is coordinated to the side chains of Glu57 and Glu61.
Takeaway
Scientists figured out what a specific protein looks like, which helps us understand how it works and how it might be used in medicine.
Methodology
The Bh-MutT gene was cloned, expressed, and purified, followed by crystallization and X-ray data collection to determine its structure.
Limitations
The study does not address the enzymatic activity of Bh-MutT on specific substrates.
Digital Object Identifier (DOI)
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