4V7I の概要
エントリーDOI | 10.2210/pdb4v7i/pdb |
関連するPDBエントリー | 3BO0 3BO1 3KC4 |
EMDBエントリー | 1484 |
分子名称 | 5S ribosomal RNA, 50S ribosomal protein L5, 50S ribosomal protein L6, ... (56 entities in total) |
機能のキーワード | ribosome-secy complex, protein translocation, cell membrane, membrane, protein transport, translocation, transmembrane, transport, repressor, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, translation regulation, trna-binding, acetylation, methylation, antibiotic resistance, transcription, transcription regulation, transcription termination, phosphoprotein, ribosome |
由来する生物種 | Escherichia coli 詳細 |
タンパク質・核酸の鎖数 | 56 |
化学式量合計 | 2233344.03 |
構造登録者 | Gumbart, J.C.,Trabuco, L.G.,Schreiner, E.,Villa, E.,Schulten, K. (登録日: 2009-10-21, 公開日: 2014-07-09, 最終更新日: 2024-02-28) |
主引用文献 | Gumbart, J.,Trabuco, L.G.,Schreiner, E.,Villa, E.,Schulten, K. Regulation of the protein-conducting channel by a bound ribosome. Structure, 17:1453-1464, 2009 Cited by PubMed Abstract: During protein synthesis, it is often necessary for the ribosome to form a complex with a membrane-bound channel, the SecY/Sec61 complex, in order to translocate nascent proteins across a cellular membrane. Structural data on the ribosome-channel complex are currently limited to low-resolution cryo-electron microscopy maps, including one showing a bacterial ribosome bound to a monomeric SecY complex. Using that map along with available atomic-level models of the ribosome and SecY, we have determined, through molecular dynamics flexible fitting (MDFF), an atomic-resolution model of the ribosome-channel complex. We characterized computationally the sites of ribosome-SecY interaction within the complex and determined the effect of ribosome binding on the SecY channel. We also constructed a model of a ribosome in complex with a SecY dimer by adding a second copy of SecY to the MDFF-derived model. The study involved 2.7-million-atom simulations over altogether nearly 50 ns. PubMed: 19913480DOI: 10.1016/j.str.2009.09.010 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (9.6 Å) |
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