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2VDA

Solution structure of the SecA-signal peptide complex

2VDA の概要
エントリーDOI10.2210/pdb2vda/pdb
関連するPDBエントリー1M6N 1TF5 1TM6 2FSF
分子名称TRANSLOCASE SUBUNIT SECA, MALTOPORIN (2 entities in total)
機能のキーワードsugar transport, protein transport, protein targeting, transmembrane, outer membrane, signal peptide, paramagnetic relaxation enhancement, translocase, ion transport, translocation, protein secretion, nucleotide-binding, seca, porin, membrane, transport, atp-binding, high molecular weight complex
由来する生物種ESCHERICHIA COLI
詳細
細胞内の位置Cell inner membrane; Peripheral membrane protein; Cytoplasmic side: P10408
Cell outer membrane ; Multi-pass membrane protein : Q8CVI4
タンパク質・核酸の鎖数2
化学式量合計96990.49
構造登録者
Gelis, I.,Bonvin, A.M.J.J.,Keramisanou, D.,Koukaki, M.,Gouridis, G.,Karamanou, S.,Economou, A.,Kalodimos, C.G. (登録日: 2007-10-01, 公開日: 2007-11-27, 最終更新日: 2024-05-15)
主引用文献Gelis, I.,Bonvin, A.M.J.J.,Keramisanou, D.,Koukaki, M.,Gouridis, G.,Karamanou, S.,Economou, A.,Kalodimos, C.G.
Structural Basis for Signal-Sequence Recognition by the Translocase Motor Seca as Determined by NMR
Cell(Cambridge,Mass.), 131:756-, 2007
Cited by
PubMed Abstract: Recognition of signal sequences by cognate receptors controls the entry of virtually all proteins to export pathways. Despite its importance, this process remains poorly understood. Here, we present the solution structure of a signal peptide bound to SecA, the 204 kDa ATPase motor of the Sec translocase. Upon encounter, the signal peptide forms an alpha-helix that inserts into a flexible and elongated groove in SecA. The mode of binding is bimodal, with both hydrophobic and electrostatic interactions mediating recognition. The same groove is used by SecA to recognize a diverse set of signal sequences. Impairment of the signal-peptide binding to SecA results in significant translocation defects. The C-terminal tail of SecA occludes the groove and inhibits signal-peptide binding, but autoinhibition is relieved by the SecB chaperone. Finally, it is shown that SecA interconverts between two conformations in solution, suggesting a simple mechanism for polypeptide translocation.
PubMed: 18022369
DOI: 10.1016/J.CELL.2007.09.039
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2vda
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2026-02-25に公開中

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