Conformational Changes in a Thermophilic Ribose-Binding Protein
Author Information
Author(s): Cuneo Matthew J, Beese Lorena S, Hellinga Homme W
Primary Institution: The Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA
Hypothesis
How do ligand-induced conformational changes differ between thermophilic and mesophilic ribose-binding proteins?
Conclusion
The study reveals that while large-scale ligand-induced changes are similar in both proteins, small-scale structural rearrangements differ significantly.
Supporting Evidence
- The T. maritima ribose-binding protein is more thermally stable than its E. coli counterpart.
- Both proteins exhibit conserved global conformational changes upon ligand binding.
- Local structural rearrangements in the ligand-binding site differ between the thermophilic and mesophilic proteins.
Takeaway
This study looks at how a protein from a heat-loving bacteria changes shape when it binds to sugar, showing that it behaves differently than a similar protein from a regular bacteria.
Methodology
The study involved biochemical characterization and X-ray crystal structure determination of the ribose-binding protein from Thermotoga maritima.
Digital Object Identifier (DOI)
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