The crystal structure of the E. coli stress protein YciF.
YciF is a protein that is up-regulated when bacteria experience stress conditions, and is highly conserved in a range of bacterial species. YciF has no known structure or biochemical function. To learn more about its potential molecular function and its role in the bacterial stress response, we solved the crystal structure of YciF at 2.0 Angstrom resolution by the multiple wavelength anomalous diffraction (MAD) technique. YciF is a dimer in solution, and forms a homodimer in the crystal asymmetric unit. The two monomers form a dimer with a molecular twofold axis, with a significant burial of solvent-accessible surface area. The protein is an all-alpha protein composed of five helices: a four-helix bundle, and a short additional helix at the dimer interface. The protein is structurally similar to portions of the diiron-containing proteins, rubrerythrin and the Bacillus anthracis Dlp-2.
Hindupur
Aditya
A
Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, Texas 77555-0647, USA.
Liu
Deqian
D
Zhao
Yonghong
Y
Bellamy
Henry D
HD
White
Mark A
MA
Fox
Robert O
RO
D000595:Amino Acid Sequence; D001408:Bacillus anthracis / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D018360:Crystallography, X-Ray / Q000379:methods*; D019281:Dimerization; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D005288:Ferredoxins / Q000737:chemistry; D006360:Heat-Shock Proteins / Q000737:chemistry*; D006422:Hemerythrin; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012416:Rubredoxins; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D005288:Ferredoxins; D006360:Heat-Shock Proteins; D006422:Hemerythrin; D008024:Ligands; D012416:Rubredoxins; C500525:YciF protein, E coli; C055857:rubrerythrins