Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription

Shuying Wang, Rhonda T. Fleming, Edwin M. Westbrook, Philip Matsumura, David B. McKay

Research output: Contribution to journalArticlepeer-review

109 Citations (Scopus)


The hetero-oligomeric complex of the FlhD and FlhC proteins (FlhDC) regulates transcription from several flagellar and non-flagellar operons in bacteria. The crystallographic structure of the Escherichia coli FlhDC complex has been solved to 3.0 Å resolution, revealing a hexameric FlhD 4FlhC2 assembly. In the complex, each FlhC protomer binds an FlhD2 dimer; the conformation of the dimer in the complex differs significantly from its conformation in the absence of FlhC. FlhC has a novel tertiary fold that includes a heretofore unrecognized zinc-binding site in which the ion is ligated by four cysteine residues. Gel shift experiments show that binding of the FlhDC complex to a cognate promoter bends the DNA by approximately 111°. The structure of the FlhDC complex is compatible with models in which a fragment of operator DNA, at least 48 base-pairs in length, wraps around the complex and bends significantly when binding.

Original languageEnglish
Pages (from-to)798-808
Number of pages11
JournalJournal of Molecular Biology
Issue number4
Publication statusPublished - 2006 Jan 27

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology


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