An alternate mode of oligomerization for E. coli SecA
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-017-11648-5.pdf
Reference68 articles.
1. Chatzi, K. E., Sardis, M. F., Economou, A. & Karamanou, S. SecA-mediated targeting and translocation of secretory proteins. Biochim. Biophys. Acta 1843, 1466–1474 (2014).
2. Collinson, I., Corey, R. A. & Allen, W. J. Channel crossing: how are proteins shipped across the bacterial plasma membrane? Philos. Trans. R. Soc. Lond. B. Biol. Sci. 370, 20150025 (2015).
3. Lycklama a Nijeholt, J. A. & Driessen, A. J. M. The bacterial Sec-translocase: structure and mechanism. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 367, 1016–1028 (2012).
4. Sardis, M. F. & Economou, A. SecA: a tale of two protomers. Mol. Microbiol. 76, 1070–1081 (2010).
5. Li, L. et al. Crystal structure of a substrate-engaged SecY protein-translocation channel. Nature 531, 395–399 (2016).
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2. Structure of the substrate-engaged SecA-SecY protein translocation machine;Nature Communications;2019-06-28
3. Direct visualization of the E. coli Sec translocase engaging precursor proteins in lipid bilayers;Science Advances;2019-06-07
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