The crystal structure of the E. coli stress protein YciF

Aditya Hindupur, Deqian Liu, Yonghong Zhao, Henry D. Bellamy, Mark A. White, Robert O. Fox

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


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 Å 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. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)2605-2611
Number of pages7
JournalProtein Science
Issue number11
StatePublished - 2006

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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