4JML

Crystal structure of the TolB(P201C)-ColicinE9 TBE peptide(A33C) complex.

4JML の概要

• エントリーDOI: 10.2210/pdb4jml/pdb
• 関連するPDBエントリー: 2ivz
• 分子名称: Protein TolB, Colicin-E9, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: protein-protein interaction, engineered disulfide, bacteriocin transport, protein transport, protein transport-toxin complex, protein transport/toxin
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46396.33

構造登録者

Wojdyla, J.A.,Klein, A.,Kleanthous, C. (登録日: 2013-03-14, 公開日: 2013-07-17, 最終更新日: 2024-11-20)

主引用文献

Housden, N.G.,Hopper, J.T.,Lukoyanova, N.,Rodriguez-Larrea, D.,Wojdyla, J.A.,Klein, A.,Kaminska, R.,Bayley, H.,Saibil, H.R.,Robinson, C.V.,Kleanthous, C.
Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF.
Science, 340:1570-1574, 2013

PubMed Abstract: 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.

PubMed: 23812713
DOI: 10.1126/science.1237864

実験手法

X-RAY DIFFRACTION (2 Å)