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2CXC

Crystal structure of archaeal transcription termination factor NusA

2CXC の概要
エントリーDOI10.2210/pdb2cxc/pdb
分子名称NusA (2 entities in total)
機能のキーワードtranscription termination, rna binding protein, archaeal nusa, kh domain, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, transcription
由来する生物種Aeropyrum pernix
タンパク質・核酸の鎖数1
化学式量合計16069.72
構造登録者
Shibata, R.,Bessho, Y.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2005-06-28, 公開日: 2005-12-28, 最終更新日: 2024-03-13)
主引用文献Shibata, R.,Bessho, Y.,Shinkai, A.,Nishimoto, M.,Fusatomi, E.,Terada, T.,Shirouzu, M.,Yokoyama, S.
Crystal structure and RNA-binding analysis of the archaeal transcription factor NusA
Biochem.Biophys.Res.Commun., 355:122-128, 2007
Cited by
PubMed Abstract: The transcription factor NusA functions in transcriptional regulation involving termination in bacteria. A NusA homolog consisting of only the two KH domains is widely conserved in archaea, but its function remains unknown. We have found that Aeropyrum pernix NusA strongly binds to a certain CU-rich sequence near a termination signal. Our crystal structure of A. pernix NusA revealed that its spatial arrangement is quite similar to that of the KH domains of bacterial NusA. Thus, we consider archaeal NusA to have retained some functions of bacterial NusA, including the ssRNA-binding ability. Remarkable structural differences between archaeal and bacterial NusA exist at the interface with RNAP, in connection with the different NusA-binding sites around the termination signals. Transcriptional termination in archaea could differ from all of the known bacterial and eukaryal mechanisms, in terms of the combination of a bacterial factor and a eukaryal-type RNAP.
PubMed: 17288993
DOI: 10.1016/j.bbrc.2007.01.119
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 2cxc
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2026-01-28に公開中

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