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          Institute: MPI für Biophysik     Collection: Abt. Strukturbiologie     Display Documents

ID: 577721.0, MPI für Biophysik / Abt. Strukturbiologie
Structure of the SecY Complex Unlocked by a Preprotein Mimic
Authors:Hizlan, Dilem; Whitehouse, Sarah; Gold, Vicki A.; Vonck, Janet; Mills, Deryck; Kühlbrandt, Werner; Collinson, Ian
Date of Publication (YYYY-MM-DD):2012
Title of Journal:Cell Reports
Journal Abbrev.:Cell Reports
Issue / Number:1
Start Page:21
End Page:28
Review Status:Peer-review
Audience:Experts Only
Abstract / Description:The Sec complex forms the core of a conserved machinery coordinating the passage of proteins across or into biological membranes. The bacterial complex SecYEG interacts with the ATPase SecA or translating ribosomes to translocate secretory and membrane proteins accordingly. A truncated preprotein competes with the physiological full- length substrate and primes the protein-channel complex for transport. We have employed electron cryomicroscopy of two-dimensional crystals to determine the structure of the complex unlocked by the preprotein. Its visualization in the native environment of the membrane preserves the active arrangement of SecYEG dimers, in which only one of the two channels is occupied by the polypeptide substrate. The signal sequence could be identified along with the corresponding conformational changes in SecY, including relocation of transmem- brane segments 2b and 7 as well as the plug, which presumably then promote channel opening. There- fore, we propose that the structure describes the translocon unlocked by preprotein and poised for protein translocation.
Free Keywords:SecY
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für Biophysik/Abteilung Strukturbiologie
External Affiliations:School of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK;
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