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Three-dimensional structure of the bacterial protein-translocation complex SecYEG

MPG-Autoren
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Breyton,  Cécile
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;
CNRS-UMR7099, IBPC, 13 rue P. et M. Curie, 75005, Paris, France;

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Haase,  Winfried
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt,  Werner       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Collinson,  Ian
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;
Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Massachusetts, 02115, Boston, USA;

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Zitation

Breyton, C., Haase, W., Rapoport, T. A., Kühlbrandt, W., & Collinson, I. (2002). Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature, 418(6898), 662-665. doi:10.1038/nature00827.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0024-DCA3-D
Zusammenfassung
Transport and membrane integration of polypeptides is carried out by specific protein complexes in the membranes of all living cells. The Sec transport path provides an essential and ubiquitous route for protein translocation. In the bacterial cytoplasmic membrane, the channel is formed by oligomers of a heterotrimeric membrane protein complex consisting of subunits SecY, SecE and SecG. In the endoplasmic reticulum membrane, the channel is formed from the related Sec61 complex. Here we report the structure of the Escherichia coli SecYEG assembly at an in-plane resolution of 8 A. The three-dimensional map, calculated from two-dimensional SecYEG crystals, reveals a sandwich of two membranes interacting through the extensive cytoplasmic domains. Each membrane is composed of dimers of SecYEG. The monomeric complex contains 15 transmembrane helices. In the centre of the dimer we observe a 16 x 25 A cavity closed on the periplasmic side by two highly tilted transmembrane helices. This may represent the closed state of the protein-conducting channel.