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 and function of the Si3 insertion integrated into the trigger loop/helix of cyanobacterial RNA polymerase.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 121, Issue 8, Page e2311480121, Year 2024
掲載日	2024年2月20日
著者	M Zuhaib Qayyum / Masahiko Imashimizu / Miron Leanca / Rishi K Vishwakarma / Amber Riaz-Bradley / Yulia Yuzenkova / Katsuhiko S Murakami /
PubMed 要旨	Cyanobacteria and evolutionarily related chloroplasts of algae and plants possess unique RNA polymerases (RNAPs) with characteristics that distinguish them from canonical bacterial RNAPs. The largest ...Cyanobacteria and evolutionarily related chloroplasts of algae and plants possess unique RNA polymerases (RNAPs) with characteristics that distinguish them from canonical bacterial RNAPs. The largest subunit of cyanobacterial RNAP (cyRNAP) is divided into two polypeptides, β'1 and β'2, and contains the largest known lineage-specific insertion domain, Si3, located in the middle of the trigger loop and spanning approximately half of the β'2 subunit. In this study, we present the X-ray crystal structure of Si3 and the cryo-EM structures of the cyRNAP transcription elongation complex plus the NusG factor with and without incoming nucleoside triphosphate (iNTP) bound at the active site. Si3 has a well-ordered and elongated shape that exceeds the length of the main body of cyRNAP, fits into cavities of cyRNAP in the absence of iNTP bound at the active site and shields the binding site of secondary channel-binding proteins such as Gre and DksA. A small transition from the trigger loop to the trigger helix upon iNTP binding results in a large swing motion of Si3; however, this transition does not affect the catalytic activity of cyRNAP due to its minimal contact with cyRNAP, NusG, or DNA. This study provides a structural framework for understanding the evolutionary significance of these features unique to cyRNAP and chloroplast RNAP and may provide insights into the molecular mechanism of transcription in specific environment of photosynthetic organisms and organelle.
リンク	Proc Natl Acad Sci U S A / PubMed:38354263 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	2.79 - 3.06 Å
構造データ	40874 8syi EMDB-40874, PDB-8syi: Cyanobacterial RNAP-EC 手法: EM (単粒子) / 解像度: 2.94 Å 42502 8urw EMDB-42502, PDB-8urw: Cyanobacterial RNA polymerase elongation complex with NusG and CTP 手法: EM (単粒子) / 解像度: 2.79 Å PDB-8emb: X-ray crystal structure of Thermosynechococcus elongatus Si3 domain of RNA polymerase RpoC2 subunit 手法: X-RAY DIFFRACTION / 解像度: 3.06 Å
化合物	ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-ZN: Unknown entry ChemComp-CTP: CYTIDINE-5'-TRIPHOSPHATE / CTP / シチジン三リン酸
由来	synechococcus elongatus (バクテリア) synthetic construct (人工物) thermosynechococcus vestitus bp-1 (バクテリア)
キーワード	TRANSCRIPTION (転写 (生物学)) / RNA polymerase (RNAポリメラーゼ) / Lineage specific insertion / trigger loop / Transcription regulation RNAP NusG cryo-EM / Transcription regulation / RNAP (RNAポリメラーゼ) / NusG / cryo-EM (低温電子顕微鏡法)