Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8PB9

Cryo-EM structure of the c-di-GMP-bound FleQ-FleN master regulator complex from Pseudomonas aeruginosa

8PB9 の概要
エントリーDOI10.2210/pdb8pb9/pdb
関連するPDBエントリー8p53
EMDBエントリー17445 17581
分子名称Transcriptional regulator FleQ, Antiactivator FleN, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one), ... (4 entities in total)
機能のキーワードbiofilm formation, c-di-gmp signaling, second messengers, bacterial secretion, gene regulation, bebps
由来する生物種Pseudomonas aeruginosa PAO1
詳細
タンパク質・核酸の鎖数5
化学式量合計197698.47
構造登録者
Torres-Sanchez, L.T.,Krasteva, P.V. (登録日: 2023-06-08, 公開日: 2023-12-13, 最終更新日: 2025-10-01)
主引用文献Torres-Sanchez, L.,Gery Sana, T.,Decossas, M.,Hashem, Y.,Krasteva, P.V.
Structures of the P. aeruginosa FleQ-FleN master regulators reveal large-scale conformational switching in motility and biofilm control.
Proc.Natl.Acad.Sci.USA, 120:e2312276120-e2312276120, 2023
Cited by
PubMed Abstract: can cause a wide array of chronic and acute infections associated with its ability to rapidly switch between planktonic, biofilm, and dispersed lifestyles, each with a specific arsenal for bacterial survival and virulence. At the cellular level, many of the physiological transitions are orchestrated by the intracellular second messenger c-di-GMP and its receptor-effector FleQ. A bacterial enhancer binding protein, FleQ acts as a master regulator of both flagellar motility and adherence factor secretion and uses remarkably different transcription activation mechanisms depending on its dinucleotide loading state, adenosine triphosphatase (ATPase) activity, interactions with polymerase sigma (σ) factors, and complexation with a second ATPase, FleN. How the FleQ-FleN tandem can exert diverse effects through recognition of a conserved FleQ binding consensus has remained enigmatic. Here, we provide cryogenic electron microscopy (cryo-EM) structures of both c-di-GMP-bound and c-di-GMP-free FleQ-FleN complexes which deepen our understanding of the proteins' (di)nucleotide-dependent conformational switching and fine-tuned roles in gene expression regulation.
PubMed: 38051770
DOI: 10.1073/pnas.2312276120
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.3 Å)
構造検証レポート
Validation report summary of 8pb9
検証レポート(詳細版)ダウンロードをダウンロード

248942

件を2026-02-11に公開中

PDB statisticsPDBj update infoContact PDBjnumon