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

Cécile Breyton (), Winfried Haase, Tom A. Rapoport, Werner Kühlbrandt and Ian Collinson ()
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Cécile Breyton: Max-Planck-Institut für Biophysik, Abteilung Strukturbiologie
Winfried Haase: Max-Planck-Institut für Biophysik, Abteilung Strukturbiologie
Tom A. Rapoport: Harvard Medical School
Werner Kühlbrandt: Max-Planck-Institut für Biophysik, Abteilung Strukturbiologie
Ian Collinson: Max-Planck-Institut für Biophysik, Abteilung Strukturbiologie

Nature, 2002, vol. 418, issue 6898, 662-665

Abstract: Abstract 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 translocation1. In the bacterial cytoplasmic membrane, the channel is formed by oligomers of a heterotrimeric membrane protein complex consisting of subunits SecY, SecE and SecG2,3. In the endoplasmic reticulum membrane, the channel is formed from the related Sec61 complex4. Here we report the structure of the Escherichia coli SecYEG assembly at an in-plane resolution of 8 Å. 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 × 25 Å cavity closed on the periplasmic side by two highly tilted transmembrane helices. This may represent the closed state of the protein-conducting channel.

Date: 2002
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DOI: 10.1038/nature00827

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