- PDB-4jml: Crystal structure of the TolB(P201C)-ColicinE9 TBE peptide(A33C) ... -
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基本情報
登録情報
データベース: PDB / ID: 4jml
タイトル
Crystal structure of the TolB(P201C)-ColicinE9 TBE peptide(A33C) complex.
要素
Colicin-E9
Protein TolB
キーワード
PROTEIN TRANSPORT/TOXIN / protein-protein interaction (タンパク質間相互作用) / engineered disulfide / bacteriocin transport / protein transport / PROTEIN TRANSPORT-TOXIN complex
機能・相同性
機能・相同性情報
extrachromosomal circular DNA / endonuclease activity / killing of cells of another organism / 加水分解酵素; エステル加水分解酵素 / defense response to bacterium / protein domain specific binding / protein-containing complex / metal ion binding 類似検索 - 分子機能
ジャーナル: Science / 年: 2013 タイトル: Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF. 著者: Nicholas G Housden / Jonathan T S Hopper / Natalya Lukoyanova / David Rodriguez-Larrea / Justyna A Wojdyla / Alexander Klein / Renata Kaminska / Hagan Bayley / Helen R Saibil / Carol V ...著者: Nicholas G Housden / Jonathan T S Hopper / Natalya Lukoyanova / David Rodriguez-Larrea / Justyna A Wojdyla / Alexander Klein / Renata Kaminska / Hagan Bayley / Helen R Saibil / Carol V Robinson / Colin Kleanthous / 要旨: Porins are β-barrel outer-membrane proteins through which small solutes and metabolites diffuse that are also exploited during cell death. We have studied how the bacteriocin colicin E9 (ColE9) ...Porins are β-barrel outer-membrane proteins through which small solutes and metabolites diffuse that are also exploited during cell death. We have studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin OmpF. Formation of the translocon involved ColE9's unstructured N-terminal domain threading in opposite directions through two OmpF subunits, capturing its target TolB on the other side of the membrane in a fixed orientation that triggers colicin import. Thus, an intrinsically disordered protein can tunnel through the narrow pores of an oligomeric porin to deliver an epitope signal to the cell to initiate cell death.