3LSJ

Crystal structure of DesT in complex with palmitoyl-CoA

Summary for 3LSJ

• Entry DOI: 10.2210/pdb3lsj/pdb
• Related: 3LSP 3LSR
• Descriptor: DesT, PALMITIC ACID, COENZYME A, ... (4 entities in total)
• Functional Keywords: transcriptional repressor, dest, tetr family, dna-binding, transcription, transcription regulation
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 50049.31

Authors

Miller, D.J.,White, S.W. (deposition date: 2010-02-12, release date: 2010-08-04, Last modification date: 2024-02-21)

Primary citation

Miller, D.J.,Zhang, Y.M.,Subramanian, C.,Rock, C.O.,White, S.W.
Structural basis for the transcriptional regulation of membrane lipid homeostasis.
Nat.Struct.Mol.Biol., 17:971-975, 2010

PubMed Abstract: DesT is a transcriptional repressor that regulates the genes that control the unsaturated:saturated fatty acid ratio available for membrane lipid synthesis. DesT bound to unsaturated acyl-CoA has a high affinity for its cognate palindromic DNA-binding site, whereas DesT bound to saturated acyl-CoA does not bind this site. Structural analyses of the DesT-oleoyl-CoA-DNA and DesT-palmitoyl-CoA complexes reveal that acyl chain shape directly influences the packing of hydrophobic core residues within the DesT ligand-binding domain. These changes are propagated to the paired DNA-binding domains via conformational changes to modulate DNA binding. These structural interpretations are supported by the in vitro and in vivo characterization of site-directed mutants. The regulation of DesT by the unsaturated:saturated ratio of acyl chains rather than the concentration of a single ligand is a paradigm for understanding transcriptional regulation of membrane lipid homeostasis.

PubMed: 20639888
DOI: 10.1038/nsmb.1847

Experimental method

X-RAY DIFFRACTION (2.3 Å)