title: FolX from Pseudomonas aeruginosa is octameric in both crystal and solution.
abstract: 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.
authors.affiliation: Institute of Infection, Immunity and Immunology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, UK.
authors.forename: Mads
authors.initials: M
authors.lastname: Gabrielsen
authors.forename: Katherine S H
authors.initials: KS
authors.lastname: Beckham
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Cogdell
authors.forename: Olwyn
authors.initials: O
authors.lastname: Byron
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: Roe
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D020134:Catalytic Domain; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D019998:Racemases and Epimerases / Q000737:chemistry* / Q000378:metabolism; D053838:Scattering, Small Angle; D012996:Solutions; D014461:Ultracentrifugation
chemical_list: D001426:Bacterial Proteins; D012996:Solutions; D019998:Racemases and Epimerases