4LY6

Nucleotide-induced asymmetry within ATPase activator ring drives s54-RNAP interaction and ATP hydrolysis

4LY6 の概要

• エントリーDOI: 10.2210/pdb4ly6/pdb
• 関連するPDBエントリー: 4LZZ
• 分子名称: Transcriptional regulator (NtrC family), [[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-tris(fluoranyl)beryllium, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: aaa+ atpase, bacterial enhancer binding protein, s54-dependent transcription activator, molecular machine, sigma54, s54-rnap, transcription regulator
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 748742.87

構造登録者

Sysoeva, T.A.,Chowdhury, S.,Guo, L.,Nixon, B.T. (登録日: 2013-07-30, 公開日: 2013-12-04, 最終更新日: 2024-02-28)

主引用文献

Sysoeva, T.A.,Chowdhury, S.,Guo, L.,Nixon, B.T.
Nucleotide-induced asymmetry within ATPase activator ring drives sigma 54-RNAP interaction and ATP hydrolysis.
Genes Dev., 27:2500-2511, 2013

PubMed Abstract: It is largely unknown how the typical homomeric ring geometry of ATPases associated with various cellular activities enables them to perform mechanical work. Small-angle solution X-ray scattering, crystallography, and electron microscopy (EM) reconstructions revealed that partial ATP occupancy caused the heptameric closed ring of the bacterial enhancer-binding protein (bEBP) NtrC1 to rearrange into a hexameric split ring of striking asymmetry. The highly conserved and functionally crucial GAFTGA loops responsible for interacting with σ54-RNA polymerase formed a spiral staircase. We propose that splitting of the ensemble directs ATP hydrolysis within the oligomer, and the ring's asymmetry guides interaction between ATPase and the complex of σ54 and promoter DNA. Similarity between the structure of the transcriptional activator NtrC1 and those of distantly related helicases Rho and E1 reveals a general mechanism in homomeric ATPases whereby complex allostery within the ring geometry forms asymmetric functional states that allow these biological motors to exert directional forces on their target macromolecules.

PubMed: 24240239
DOI: 10.1101/gad.229385.113

実験手法

X-RAY DIFFRACTION (3.6 Å)