3LSJ

Crystal structure of DesT in complex with palmitoyl-CoA

3LSJ の概要

• エントリーDOI: 10.2210/pdb3lsj/pdb
• 関連するPDBエントリー: 3LSP 3LSR
• 分子名称: DesT, PALMITIC ACID, COENZYME A, ... (4 entities in total)
• 機能のキーワード: transcriptional repressor, dest, tetr family, dna-binding, transcription, transcription regulation
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50049.31

構造登録者

Miller, D.J.,White, S.W. (登録日: 2010-02-12, 公開日: 2010-08-04, 最終更新日: 2024-02-21)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)