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1 Ontario Center for Structural Proteomics, University Health Network, University of Toronto, Toronto, Ontario M5G 1L7, Canada
2 Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6, Canada
(RECEIVED February 13, 2006; FINAL REVISION February 13, 2006; ACCEPTED February 22, 2006)
The crystal structure of Escherichia coli PhnF C-terminal domain (C-PhnF) was solved at 1.7 Å resolution by the single wavelength anomalous dispersion (SAD) method. The PhnF protein belongs to the HutC subfamily of the large GntR transcriptional regulator family. Members of this family share similar N-terminal DNA-binding domains, but are divided into four subfamilies according to their heterogenic C-terminal domains, which are involved in effector binding and oligomerization. The C-PhnF structure provides for the first time the scaffold of this domain for the HutC subfamily, which covers about 31% of GntR-like regulators. The structure represents a mixture of 
-helices and 
-strands, with a six-stranded antiparallel -sheet at the core. C-PhnF monomers form a dimer by establishing interdomain eight-strand -sheets that include core antiparallel and N-terminal two-strand parallel -sheets from each monomer. C-PhnF shares strong structural similarity with the chorismate lyase fold, which features a buried active site locked behind two helix-turn-helix loops. The structural comparison of the C-PhnF and UbiC proteins allows us to propose that a similar site in the PhnF structure is adapted for effector binding.
Keywords: effector binding domain; transcriptional regulator; HutC; PhnF; chorismate lyase fold; GntR family
Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.062146906.
Abbreviations: C-PhnF, C-terminal domain of PhnF; C-P, carbon-phosphate; DB, DNA binding domain; HTH, helix-turn-helix; SAD, single wavelength anomalous dispersion; Pn, Phosphonates; TEV protease, Tobacco Etch Virus protease; wHTH, winged helix-turn-helix.
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