6EN8

SaFadR in complex with dsDNA

6EN8 の概要

• エントリーDOI: 10.2210/pdb6en8/pdb
• 関連するPDBエントリー: 5MWR 6EL2
• 分子名称: Transcriptional regulator TetR family, DNA (5'-D(*GP*TP*CP*GP*AP*CP*TP*CP*AP*AP*AP*AP*AP*TP*CP*AP*AP*GP*TP*AP*G)-3'), DNA (5'-D(*CP*TP*AP*CP*TP*TP*GP*AP*TP*TP*TP*TP*TP*GP*AP*GP*TP*CP*GP*AP*C)-3'), ... (4 entities in total)
• 機能のキーワード: transcription factor, complex, dsdna, transcription
• 由来する生物種: Sulfolobus acidocaldarius; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 169764.98

構造登録者

Valegard, K. (登録日: 2017-10-04, 公開日: 2018-10-31, 最終更新日: 2024-10-16)

主引用文献

Wang, K.,Sybers, D.,Maklad, H.R.,Lemmens, L.,Lewyllie, C.,Zhou, X.,Schult, F.,Brasen, C.,Siebers, B.,Valegard, K.,Lindas, A.C.,Peeters, E.
A TetR-family transcription factor regulates fatty acid metabolism in the archaeal model organism Sulfolobus acidocaldarius.
Nat Commun, 10:1542-1542, 2019

PubMed Abstract: Fatty acid metabolism and its regulation are known to play important roles in bacteria and eukaryotes. By contrast, although certain archaea appear to metabolize fatty acids, the regulation of the underlying pathways in these organisms remains unclear. Here, we show that a TetR-family transcriptional regulator (FadR) is involved in regulation of fatty acid metabolism in the crenarchaeon Sulfolobus acidocaldarius. Functional and structural analyses show that FadR binds to DNA at semi-palindromic recognition sites in two distinct stoichiometric binding modes depending on the operator sequence. Genome-wide transcriptomic and chromatin immunoprecipitation analyses demonstrate that the protein binds to only four genomic sites, acting as a repressor of a 30-kb gene cluster comprising 23 open reading frames encoding lipases and β-oxidation enzymes. Fatty acyl-CoA molecules cause dissociation of FadR binding by inducing conformational changes in the protein. Our results indicate that, despite its similarity in overall structure to bacterial TetR-family FadR regulators, FadR displays a different acyl-CoA binding mode and a distinct regulatory mechanism.

PubMed: 30948713
DOI: 10.1038/s41467-019-09479-1

実験手法

X-RAY DIFFRACTION (3.29 Å)