FolX from Pseudomonas aeruginosa is octameric in both crystal and solution

FEBS Lett. 2012 Apr 24;586(8):1160-5. doi: 10.1016/j.febslet.2012.03.031. Epub 2012 Mar 24.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Catalytic Domain
  • Circular Dichroism
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Pseudomonas aeruginosa / enzymology*
  • Racemases and Epimerases / chemistry*
  • Racemases and Epimerases / metabolism
  • Scattering, Small Angle
  • Solutions
  • Ultracentrifugation

Substances

  • Bacterial Proteins
  • Solutions
  • Racemases and Epimerases