EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Structure of the giant RNA polymerase ejected from coliphage N4.
ジャーナル・号・ページ	Res Sq, Year 2025
掲載日	2025年10月21日
著者	Nathan F Bellis / Ravi K Lokareddy / Mikhail Pavlenok / Stephanie L Cooper Horton / James L Kizziah / Francesca Forti / David A Schneider / Michael Niederweis / Federica Briani / Gino Cingolani /
PubMed 要旨	are widespread prokaryotic viruses that encapsidate a giant (~3,500-residue) virion-associated RNA polymerase (vRNAP). During infection, vRNAP is expelled into Gram-negative bacteria, along with two ... are widespread prokaryotic viruses that encapsidate a giant (~3,500-residue) virion-associated RNA polymerase (vRNAP). During infection, vRNAP is expelled into Gram-negative bacteria, along with two additional ejection proteins, to assemble a transient DNA-ejectosome that becomes transcriptionally active, initiating viral replication. Here, we present an integrative structural analysis of the coliphage N4 vRNAP (gp50). We find that this 383 kDa enzyme is a multi-domain, single-chain RNA polymerase, structurally distinct from both compact single-chain RNAPs and large multi-subunit holoenzymes. vRNAP is composed of loosely connected domains and exhibits an intramolecular mode of allosteric regulation through its C-terminal domain. Comparative analysis of intact and genome-released virions identified gp51, which forms an outer-membrane complex, and gp52, which assembles a periplasmic tunnel. These proteins generate heterogeneous pores that facilitate the release of vRNAP. We further uncover a signaling hub in the phage tail, composed of the receptor-binding protein, tail tube, and tail plug, that detects receptor engagement and orchestrates the release of ejection proteins. We propose that the beads-on-a-string architecture of vRNAP enables the translocation of megadalton-scale protein complexes through the ~35 Å channel formed by the tail and ejection proteins. These findings establish N4 as a distinctive model for protein translocation through biological channels.
リンク	Res Sq / PubMed:41282253 / PubMed Central
手法	EM (単粒子)
解像度	2.61 - 4.3 Å
構造データ	71768 9pnq EMDB-71768, PDB-9pnq: N4 vRNAP gp50 - Isolated RNAP Domain 手法: EM (単粒子) / 解像度: 2.61 Å 71769 9pnr EMDB-71769, PDB-9pnr: N4 vRNAP gp50 - Closed Complex 手法: EM (単粒子) / 解像度: 2.8 Å 71771 9pnt EMDB-71771, PDB-9pnt: N4 vRNAP gp50 - open complex 手法: EM (単粒子) / 解像度: 4.3 Å 71773 9pnv EMDB-71773, PDB-9pnv: N4 vRNAP gp50 bound to P1 Promoter - Isolated RNAP Domain 手法: EM (単粒子) / 解像度: 2.8 Å 71774 9pnw EMDB-71774, PDB-9pnw: N4 vRNAP gp50 bound to P1 promoter - closed complex 手法: EM (単粒子) / 解像度: 2.9 Å 72877 9yf5 EMDB-72877, PDB-9yf5: N4 Empty Particle C6 Tail 手法: EM (単粒子) / 解像度: 3.65 Å 72880 9yf8 EMDB-72880, PDB-9yf8: N4 Full Virion Portal 手法: EM (単粒子) / 解像度: 2.9 Å
由来	escherichia phage n4 (ファージ)
キーワード	VIRAL PROTEIN / TRANSFERASE / Single Subunit RNA Polymerase / Bacteriophage Ejection Protein / single-subunit RNAP polymerase / dodecamer / bacteriophage portal