1h9t

From Proteopedia

Revision as of 14:21, 20 November 2007

FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI IN COMPLEX WITH FADB OPERATOR

Overview

FadR is an acyl-CoA-responsive transcription factor, regulating fatty acid, biosynthetic and degradation genes in Escherichia coli. The apo-protein, binds DNA as a homodimer, an interaction that is disrupted by binding of, acyl-COA: The recently described structure of apo-FadR shows a DNA binding, domain coupled to an acyl-CoA binding domain with a novel fold, but does, not explain how binding of the acyl-CoA effector molecule > 30 A away from, the DNA binding site affects transcriptional regulation. Here, we describe, the structures of the FadR-operator and FadR- myristoyl-CoA binary, complexes. The FadR-DNA complex reveals a novel winged helix-turn-helix, protein-DNA interaction, involving sequence-specific contacts from the, wing to the minor groove. Binding of acyl-CoA results in dramatic, conformational changes throughout the protein, with backbone shifts up to, 4.5 A. The net effect is a rearrangement of the DNA binding domains in the, dimer, resulting in a change of 7.2 A in separation of the DNA recognition, helices and the loss of DNA binding, revealing the molecular basis of, acyl-CoA-responsive regulation.

About this Structure

1H9T is a Single protein structure of sequence from Escherichia coli with CL and AU as ligands. Full crystallographic information is available from OCA.

Reference

The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR., van Aalten DM, DiRusso CC, Knudsen J, EMBO J. 2001 Apr 17;20(8):2041-50. PMID:11296236

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