Dynamic structure of the translocon SecYEG in membrane: direct single molecule observations
Raghavendar Reddy Sanganna Gari1, Nathan C Frey1, Chunfeng Mao2
1Departments of Physics and Astronomy, Columbia, Missouri 65211.
Abstract:
Purified SecYEG was reconstituted into liposomes and studied in near-native conditions using atomic force microscopy. These SecYEG proteoliposomes were active in translocation assays. Changes in the structure of SecYEG as a function of time were directly visualized. The dynamics observed were significant in magnitude (∼1-10 Å) and were attributed to the two large loops of SecY linking transmembrane helices 6-7 and 8-9. In addition, we identified a distribution between monomers and dimers of SecYEG as well as a smaller population of higher order oligomers. This work provides a new vista of the flexible and dynamic structure of SecYEG, an intricate and vital membrane protein.
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