Structure of the SecY complex unlocked by a preprotein mimic.

Cell Reports
Dilem HizlanIan Collinson

Abstract

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 transmembrane segments 2b and 7 as well as the plug, which presumably then promote channel opening. Therefore, we propose that the structure describes the translocon unlocked by preprotein and poised for protein translocation.

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Citations

Oct 23, 2012·Cell Reports·Bin Zhang, Thomas F Miller
Dec 28, 2012·Proceedings of the National Academy of Sciences of the United States of America·Anna Rychkova, Arieh Warshel
Jul 3, 2013·Proceedings of the National Academy of Sciences of the United States of America·Chunfeng MaoLinda L Randall
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Methods Mentioned

BETA
X-ray
electron microscopy
NMR
electron cryomicroscopy
optical diffraction

Software Mentioned

2dx
COOT
MAPROT
PyMOL Molecular Graphics System
ORIGTILTK
SecYEG
PyMOL
OVERLAPMAP
image
MRC

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