6ITC
Structure of a substrate engaged SecA-SecY protein translocation machine
6ITC の概要
エントリーDOI | 10.2210/pdb6itc/pdb |
EMDBエントリー | 9731 |
分子名称 | Protein translocase subunit SecA, ADENOSINE-5'-DIPHOSPHATE, (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE, ... (11 entities in total) |
機能のキーワード | seca, secy, translocation, cryo-em, protein transport |
由来する生物種 | Bacillus subtilis (strain 168) 詳細 |
タンパク質・核酸の鎖数 | 7 |
化学式量合計 | 204075.55 |
構造登録者 | Ma, C.Y.,Wu, X.F.,Sun, D.J.,Park, E.Y.,Rapoport, T.A.,Gao, N.,Long, L. (登録日: 2018-11-21, 公開日: 2019-06-12, 最終更新日: 2023-11-15) |
主引用文献 | Ma, C.,Wu, X.,Sun, D.,Park, E.,Catipovic, M.A.,Rapoport, T.A.,Gao, N.,Li, L. Structure of the substrate-engaged SecA-SecY protein translocation machine. Nat Commun, 10:2872-2872, 2019 Cited by PubMed Abstract: The Sec61/SecY channel allows the translocation of many proteins across the eukaryotic endoplasmic reticulum membrane or the prokaryotic plasma membrane. In bacteria, most secretory proteins are transported post-translationally through the SecY channel by the SecA ATPase. How a polypeptide is moved through the SecA-SecY complex is poorly understood, as structural information is lacking. Here, we report an electron cryo-microscopy (cryo-EM) structure of a translocating SecA-SecY complex in a lipid environment. The translocating polypeptide chain can be traced through both SecA and SecY. In the captured transition state of ATP hydrolysis, SecA's two-helix finger is close to the polypeptide, while SecA's clamp interacts with the polypeptide in a sequence-independent manner by inducing a short β-strand. Taking into account previous biochemical and biophysical data, our structure is consistent with a model in which the two-helix finger and clamp cooperate during the ATPase cycle to move a polypeptide through the channel. PubMed: 31253804DOI: 10.1038/s41467-019-10918-2 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.45 Å) |
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