4pdk | pdb_00004pdk

FadR, Fatty Acid Responsive Transcription Factor from Vibrio cholerae, in Complex with oleoyl-CoA

spinqualitylabelsall models 4pdk, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pdk is a 2 chain structure with sequence from Vibrio cholerae O1 biovar El Tor str. N16961. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 3VV Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FADR_VIBCH Multifunctional regulator of fatty acid metabolism. Publication Abstract from PubMed FadR is a master regulator of fatty acid metabolism and influences virulence in certain members of Vibrionaceae. Among FadR homologues of the GntR family, the Vibrionaceae protein is unusual in that it contains a C-terminal 40-residue insertion. Here we report the structure of Vibrio cholerae FadR (VcFadR) alone, bound to DNA, and in the presence of a ligand, oleoyl-CoA. Whereas Escherichia coli FadR (EcFadR) contains only one acyl-CoA-binding site in each monomer, crystallographic and calorimetric data indicate that VcFadR has two. One of the binding sites resembles that of EcFadR, whereas the other, comprised residues from the insertion, has not previously been observed. Upon ligand binding, VcFadR undergoes a dramatic conformational change that would more fully disrupt DNA binding than EcFadR. These findings suggest that the ability to bind and respond to an additional ligand allows FadR from Vibrionaceae to function as a more efficient regulator. The 40-residue insertion in Vibrio cholerae FadR facilitates binding of an additional fatty acyl-CoA ligand.,Shi W, Kovacikova G, Lin W, Taylor RK, Skorupski K, Kull FJ Nat Commun. 2015 Jan 21;6:6032. doi: 10.1038/ncomms7032. PMID:25607896 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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