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The crystal structure of the E. coli stress protein YciF

¹ Department of Biochemistry and Molecular Biology and The Sealy Center for Structural Biology & Molecular Biophysics, The University of Texas Medical Branch, Galveston, Texas 77555-0647, USA
² Center for Advanced Microstructures and Devices, Louisiana State University, Baton Rouge, Louisiana 70806, USA

(RECEIVED April 27, 2006; FINAL REVISION July 19, 2006; ACCEPTED July 20, 2006)

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.

⁴ These authors contributed equally to this work.

Reprint requests to: Robert O. Fox, Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, 301 University Blvd., Mail Route 0647, Galveston, TX 77555-0647, USA; e-mail: fox{at}bloch.utmb.edu; fax: (409) 747-4745.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.062307706.

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