2avu
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(New page: 200px<br /><applet load="2avu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2avu, resolution 3.00Å" /> '''Structure of the Esc...)
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Revision as of 06:16, 21 November 2007
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Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription
Overview
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.
About this Structure
2AVU is a Protein complex structure of sequences from Escherichia coli with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription., Wang S, Fleming RT, Westbrook EM, Matsumura P, McKay DB, J Mol Biol. 2006 Jan 27;355(4):798-808. Epub 2005 Nov 22. PMID:16337229
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