X-ray structure of a protein-conducting channel

Bert van den Berg, William M. Clemons, Ian Collinson, Yorgo Modis, Enno Hartmann, Stephen C. Harrison and Tom A. Rapoport ()
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Bert van den Berg: Harvard Medical School
William M. Clemons: Harvard Medical School
Ian Collinson: Max Planck Institute of Biophysics
Yorgo Modis: Children's Hospital and Harvard Medical School
Enno Hartmann: University Luebeck, Institute for Biology
Stephen C. Harrison: Children's Hospital and Harvard Medical School
Tom A. Rapoport: Harvard Medical School

Nature, 2004, vol. 427, issue 6969, 36-44

Abstract: Abstract A conserved heterotrimeric membrane protein complex, the Sec61 or SecY complex, forms a protein-conducting channel, allowing polypeptides to be transferred across or integrated into membranes. We report the crystal structure of the complex from Methanococcus jannaschii at a resolution of 3.2 Å. The structure suggests that one copy of the heterotrimer serves as a functional translocation channel. The α-subunit has two linked halves, transmembrane segments 1–5 and 6–10, clamped together by the γ-subunit. A cytoplasmic funnel leading into the channel is plugged by a short helix. Plug displacement can open the channel into an ‘hourglass’ with a ring of hydrophobic residues at its constriction. This ring may form a seal around the translocating polypeptide, hindering the permeation of other molecules. The structure also suggests mechanisms for signal-sequence recognition and for the lateral exit of transmembrane segments of nascent membrane proteins into lipid, and indicates binding sites for partners that provide the driving force for translocation.

Date: 2004
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DOI: 10.1038/nature02218

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