- EMDB-9731: Structure of a substrate engaged SecA-SecY protein translocation ... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-9731
タイトル
Structure of a substrate engaged SecA-SecY protein translocation machine
マップデータ
試料
複合体: SecA-SecY complex
タンパク質・ペプチド: x 7種
リガンド: x 4種
キーワード
SecA / SecY / Translocation / Cryo-EM / PROTEIN TRANSPORT
機能・相同性
機能・相同性情報
outer membrane protein complex / protein-exporting ATPase activity / cell envelope Sec protein transport complex / monoatomic ion transmembrane transporter activity / protein-secreting ATPase / protein transport by the Sec complex / intracellular protein transmembrane transport / detection of virus / outer membrane / protein import ...outer membrane protein complex / protein-exporting ATPase activity / cell envelope Sec protein transport complex / monoatomic ion transmembrane transporter activity / protein-secreting ATPase / protein transport by the Sec complex / intracellular protein transmembrane transport / detection of virus / outer membrane / protein import / signal sequence binding / SRP-dependent cotranslational protein targeting to membrane, translocation / porin activity / pore complex / protein secretion / protein transmembrane transporter activity / protein targeting / monoatomic ion transport / bioluminescence / generation of precursor metabolites and energy / cell outer membrane / outer membrane-bounded periplasmic space / symbiont entry into host cell / membrane raft / DNA damage response / ATP binding / identical protein binding / membrane / metal ion binding / plasma membrane / cytosol 類似検索 - 分子機能
Outer membrane protein OmpA-like, transmembrane domain / Outer membrane protein, OmpA / OmpA-like transmembrane domain / SecE subunit of protein translocation complex, bacterial-like / SecE superfamily / SEC-C motif / SEC-C motif / SecA P-loop domain / SecA, C-terminal helicase domain / Protein translocase subunit SecA ...Outer membrane protein OmpA-like, transmembrane domain / Outer membrane protein, OmpA / OmpA-like transmembrane domain / SecE subunit of protein translocation complex, bacterial-like / SecE superfamily / SEC-C motif / SEC-C motif / SecA P-loop domain / SecA, C-terminal helicase domain / Protein translocase subunit SecA / SecA DEAD-like, N-terminal / SecA Wing/Scaffold / SecA, preprotein cross-linking domain / SecA motor DEAD / SecA conserved site / SecA, Wing/Scaffold superfamily / SecA, preprotein cross-linking domain superfamily / SecA preprotein cross-linking domain / SecA Wing and Scaffold domain / SecA DEAD-like domain / SecA family signature. / SecA family profile. / SecA DEAD-like domain / SecA preprotein cross-linking domain / Outer membrane protein, OmpA-like, conserved site / Protein translocase subunit SecY / OmpA-like domain. / Outer membrane protein, bacterial / OmpA-like domain superfamily / OmpA family / OmpA-like domain / OmpA-like domain profile. / Protein secE/sec61-gamma signature. / Protein secY signature 1. / Protein secY signature 2. / SecE/Sec61-gamma subunits of protein translocation complex / Protein translocase complex, SecE/Sec61-gamma subunit / SecY/SEC61-alpha family / SecY domain superfamily / SecY conserved site / SecY / Outer membrane protein/outer membrane enzyme PagP, beta-barrel / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性
Protein translocase subunit SecE / Protein translocase subunit SecY / Outer membrane protein A / Protein translocase subunit SecA / Green fluorescent protein 類似検索 - 構成要素
ジャーナル: Nat Commun / 年: 2019 タイトル: Structure of the substrate-engaged SecA-SecY protein translocation machine. 著者: Chengying Ma / Xiaofei Wu / Dongjie Sun / Eunyong Park / Marco A Catipovic / Tom A Rapoport / Ning Gao / Long Li / 要旨: 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 ...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.