1HW2

FADR-DNA COMPLEX: TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ECHERICHIA COLI

Summary for 1HW2

• Entry DOI: 10.2210/pdb1hw2/pdb
• Related: 1HW1
• Descriptor: 5'-D(*CP*GP*AP*TP*CP*TP*GP*GP*TP*CP*CP*GP*AP*CP*CP*AP*GP*AP*TP*GP*CP*T)-3', 5'-D(*G*CP*AP*TP*CP*TP*GP*GP*TP*CP*GP*GP*AP*CP*CP*AP*GP*AP*TP*CP*GP*A)-3', FATTY ACID METABOLISM REGULATOR PROTEIN, ... (4 entities in total)
• Functional Keywords: helix-turn-helix, helix bundle, protein-dna complex, transcription-dna complex, transcription/dna
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (Potential): P0A8V6
• Total number of polymer chains: 4
• Total formula weight: 67535.18

Authors

Xu, Y.,Heath, R.J.,Li, Z.,Rock, C.O.,White, S.W. (deposition date: 2001-01-09, release date: 2001-01-22, Last modification date: 2024-04-03)

Primary citation

Xu, Y.,Heath, R.J.,Li, Z.,Rock, C.O.,White, S.W.
The FadR.DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli.
J.Biol.Chem., 276:17373-17379, 2001

PubMed Abstract: In Escherichia coli, the expression of fatty acid metabolic genes is controlled by the transcription factor, FadR. The affinity of FadR for DNA is controlled by long chain acyl-CoA molecules, which bind to the protein and modulate gene expression. The crystal structure of FadR reveals a two domain dimeric molecule where the N-terminal domains bind DNA, and the C-terminal domains bind acyl-CoA. The DNA binding domain has a winged-helix motif, and the C-terminal domain resembles the sensor domain of the Tet repressor. The FadR.DNA complex reveals how the protein interacts with DNA and specifically recognizes a palindromic sequence. Structural and functional similarities to the Tet repressor and the BmrR transcription factors suggest how the binding of the acyl-CoA effector molecule to the C-terminal domain may affect the DNA binding affinity of the N-terminal domain. We suggest that the binding of acyl-CoA disrupts a buried network of charged and polar residues in the C-terminal domain, and the resulting conformational change is transmitted to the N-terminal domain via a domain-spanning alpha-helix.

PubMed: 11279025
DOI: 10.1074/jbc.M100195200

Experimental method

X-RAY DIFFRACTION (3.25 Å)