Structure of fructose bisphosphate aldolase from Bartonella henselae bound to fructose 1,6-bisphosphate
2011
Structure of Fructose Bisphosphate Aldolase from Bartonella Henselae
publication
Evidence: high
Author Information
Author(s): Anna Gardberg, Jan Abendroth, Janhavi Bhandari, Banumathi Sankaran, Bart Staker
Primary Institution: Emerald BioStructures
Conclusion
The crystal structure of fructose bisphosphate aldolase from B. henselae was determined in complex with its reactant at 2.35 Å resolution.
Supporting Evidence
- Fructose bisphosphate aldolase catalyzes the cleavage of fructose 1,6-bisphosphate into glyceraldehyde 3-phosphate and dihydroxyacetone phosphate.
- The structure shares the typical barrel tertiary structure and tetrameric quaternary structure reported for previous FBPA structures.
- Crystallization in the presence of the substrate was necessary to obtain well-diffracting crystals.
Takeaway
Scientists studied a protein from a germ that can make people sick, and they found out how it works by looking at its structure.
Methodology
The enzyme was expressed in E. coli, purified, and crystallized in the presence of its substrate for X-ray crystallography.
Limitations
The study primarily focuses on the structure and does not address functional implications in detail.
Digital Object Identifier (DOI)
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