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Publication Abstract from PubMed

FolX encodes an epimerase that forms one step of the tetrahydrofolate biosynthetic pathway, which is of interest as it is an established target for important drugs. Here we report the crystal structure of FolX from the bacterial opportunistic pathogen Pseudomonas aeruginosa, as well as a detailed analysis of the protein in solution, using analytical ultracentrifugation (AUC) and small-angle X-ray scattering (SAXS). In combination, these techniques confirm that the protein is an octamer both in the crystal structure, and in solution. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: FolX and FolXbind by x-ray crystallography (View interaction) FolX and FolXbind by cosedimentation in solution (View interaction) FolX and FolXbind by x ray scattering (View interaction).

FolX from Pseudomonas aeruginosa is octameric in both crystal and solution.,Gabrielsen M, Beckham KS, Cogdell RJ, Byron O, Roe AJ FEBS Lett. 2012 Apr 24;586(8):1160-5. Epub 2012 Mar 24. PMID:22575651^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.