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1SMY

Structural basis for transcription regulation by alarmone ppGpp

1SMY の概要
エントリーDOI10.2210/pdb1smy/pdb
関連するPDBエントリー1IW7
分子名称DNA-directed RNA polymerase alpha chain, DNA-directed RNA polymerase beta chain, DNA-directed RNA polymerase beta' chain, ... (9 entities in total)
機能のキーワードrna polymerase holoenzyme, guanosine-tetraphosphate, ppgpp, transcription regulation, riken structural genomics/proteomics initiative, rsgi, structural genomics, transferase
由来する生物種Thermus thermophilus
詳細
タンパク質・核酸の鎖数12
化学式量合計863537.34
構造登録者
主引用文献Artsimovitch, I.,Patlan, V.,Sekine, S.,Vassylyeva, M.N.,Hosaka, T.,Ochi, K.,Yokoyama, S.,Vassylyev, D.G.
Structural basis for transcription regulation by alarmone ppGpp
Cell(Cambridge,Mass.), 117:299-310, 2004
Cited by
PubMed Abstract: Guanosine-tetraphosphate (ppGpp) is a major regulator of stringent control, an adaptive response of bacteria to amino acid starvation. The 2.7 A resolution structure of the Thermus thermophilus RNA polymerase (RNAP) holoenzyme in complex with ppGpp reveals that ppGpp binds to the same site near the active center in both independent RNAP molecules in the crystal but in strikingly distinct orientations. Binding is symmetrical with respect to the two diphosphates of ppGpp and is relaxed with respect to the orientation of the nucleotide base. Different modes of ppGpp binding are coupled with asymmetry of the active site configurations. The results suggest that base pairing of ppGpp with cytosines in the nontemplate DNA strand might be an essential component of transcription control by ppGpp. We present experimental evidence highlighting the importance of base-specific contacts between ppGpp and specific cytosine residues during both transcription initiation and elongation.
PubMed: 15109491
DOI: 10.1016/S0092-8674(04)00401-5
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.7 Å)
構造検証レポート
Validation report summary of 1smy
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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