1EK9

2.1A X-RAY STRUCTURE OF TOLC: AN INTEGRAL OUTER MEMBRANE PROTEIN AND EFFLUX PUMP COMPONENT FROM ESCHERICHIA COLI

1EK9 の概要

• エントリーDOI: 10.2210/pdb1ek9/pdb
• 分子名称: OUTER MEMBRANE PROTEIN TOLC (2 entities in total)
• 機能のキーワード: integral membrane protein, alpha helical barrel, beta barrel, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: P02930
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 141714.94

構造登録者

Koronakis, V.,Sharff, A.J.,Koronakis, E.,Luisi, B.,Hughes, C. (登録日: 2000-03-07, 公開日: 2000-06-28, 最終更新日: 2024-11-13)

主引用文献

Koronakis, V.,Sharff, A.,Koronakis, E.,Luisi, B.,Hughes, C.
Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export.
Nature, 405:914-919, 2000

PubMed Abstract: Diverse molecules, from small antibacterial drugs to large protein toxins, are exported directly across both cell membranes of gram-negative bacteria. This export is brought about by the reversible interaction of substrate-specific inner-membrane proteins with an outer-membrane protein of the TolC family, thus bypassing the intervening periplasm. Here we report the 2.1-A crystal structure of TolC from Escherichia coli, revealing a distinctive and previously unknown fold. Three TolC protomers assemble to form a continuous, solvent-accessible conduit--a 'channel-tunnel' over 140 A long that spans both the outer membrane and periplasmic space. The periplasmic or proximal end of the tunnel is sealed by sets of coiled helices. We suggest these could be untwisted by an allosteric mechanism, mediated by protein-protein interactions, to open the tunnel. The structure provides an explanation of how the cell cytosol is connected to the external environment during export, and suggests a general mechanism for the action of bacterial efflux pumps.

PubMed: 10879525
DOI: 10.1038/35016007

実験手法

X-RAY DIFFRACTION (2.1 Å)