Structure of Aldose Reductase from Giardia lamblia
Author Information
Author(s): Ferrell M., Abendroth J., Zhang Y., Sankaran B., Edwards T. E., Staker B. L., Van Voorhis W. C., Stewart L. J., Myler P. J.
Primary Institution: Seattle Structural Genomics Center for Infectious Disease
Conclusion
The structure of G. lamblia aldose reductase was solved to a resolution of 1.75 Å, revealing conservation in the active site and anion-binding pocket with mammalian structures, while showing divergence in the specificity pocket.
Supporting Evidence
- The aldose reductase from G. lamblia adopts a TIM-barrel fold.
- The structure was solved to a resolution of 1.75 Å.
- G. lamblia aldose reductase shows 44% sequence identity with human aldose reductase.
Takeaway
Scientists figured out the shape of a protein from a tiny parasite that causes diarrhea. This helps us understand how it works and could lead to new medicines.
Methodology
The aldose reductase was expressed in E. coli, purified, and its crystal structure was determined using X-ray diffraction.
Limitations
The study did not resolve a flexible loop involved in solvent sequestration of NADP+.
Digital Object Identifier (DOI)
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