Structure of FocB: a member of a family of transcription factors regulating fimbrial adhesin expression in uropathogenic Escherichia coli
2010 (English)In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 277, no 16, 3368-3381 p.Article in journal (Refereed) Published
In uropathogenic Escherichia coli, UPEC, different types of fimbriae are expressed in order to mediate interactions with host tissue. FocB belongs to the PapB family of transcription factors involved in the regulation of fimbriae gene clusters. Recent findings suggest that members from this family of proteins may form different protein-protein complexes and that they may exert both positive and negative effects on transcription of fimbriae genes. To elucidate the detailed function of FocB, we have determined its crystal structure at 1.4 Å resolution. FocB is an all alpha helical structure with a helix-turn-helix (HTH) motif. Interestingly, conserved residues important for DNA-binding are not located in the recognition helix of the HTH-motif, but in the preceding helix. Results from protein-DNA binding studies indicated that FocB interacts with minor groove of its cognate DNA, which also points to a DNA-interaction unusual for this motif. Packing interactions in the crystals gave two plausible dimerization interfaces. Conserved residues known to be important for protein oligomerization are present at both interfaces, suggesting that both sites play a role in a functional FocB protein.
Place, publisher, year, edition, pages
Wiley , 2010. Vol. 277, no 16, 3368-3381 p.
fimbriae, FocB, repressor protein, uropathogenic Escherichia coli, X-ray crystallography
Research subject Biochemistry
IdentifiersURN: urn:nbn:se:umu:diva-27755DOI: 10.1111/j.1742-4658.2010.07742.xISI: 000280631300010OAI: oai:DiVA.org:umu-27755DiVA: diva2:277504