2AVU

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

Summary for 2AVU

• Entry DOI: 10.2210/pdb2avu/pdb
• Descriptor: Transcriptional activator flhD, Flagellar transcriptional activator flhC, ZINC ION (3 entities in total)
• Functional Keywords: c4-type zinc finger, transcription activator
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A8S9; Cytoplasm (Probable): P0ABY7
• Total number of polymer chains: 6
• Total formula weight: 96642.53

Authors

Wang, S.,Fleming, R.T.,Westbrook, E.M.,Matsumura, P.,McKay, D.B. (deposition date: 2005-08-30, release date: 2005-12-13, Last modification date: 2024-02-14)

Primary citation

Wang, S.,Fleming, R.T.,Westbrook, E.M.,Matsumura, P.,McKay, D.B.
Structure of the Escherichia coli FlhDC Complex, a Prokaryotic Heteromeric Regulator of Transcription.
J.Mol.Biol., 355:798-808, 2006

PubMed Abstract: 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 A resolution, revealing a hexameric FlhD4FlhC2 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 degrees . 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.

PubMed: 16337229
DOI: 10.1016/j.jmb.2005.11.020

Experimental method

X-RAY DIFFRACTION (3 Å)