Baker, Matthew A B and Hynson, Robert M G and Ganuelas, Lorraine A and Mohammadi, Nasim Shah and Liew, Chu Wai and Rey, Anthony A and Duff, Anthony P and Whitten, Andrew E and Jeffries, Cy M and Delalez, Nicolas J and Morimoto, Yusuke V and Stock, Daniela and Armitage, Judith P and Turberfield, Andrew J and Namba, Keiichi and Berry, Richard M and Lee, Lawrence K (2016) Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor. Nature Structural & Molecular Biology, 23 (3). pp.197-203. ISSN 1545-9985 (N/A)
Full text not available from this repository.Abstract
Large protein complexes assemble spontaneously, yet their subunits do not prematurely form unwanted aggregates. This paradox is epitomized in the bacterial flagellar motor, a sophisticated rotary motor and sensory switch consisting of hundreds of subunits. Here we demonstrate that Escherichia coli FliG, one of the earliest-assembling flagellar motor proteins, forms ordered ring structures via domain-swap polymerization, which in other proteins has been associated with uncontrolled and deleterious protein aggregation. Solution structural data, in combination with in vivo biochemical cross-linking experiments and evolutionary covariance analysis, revealed that FliG exists predominantly as a monomer in solution but only as domain-swapped polymers in assembled flagellar motors. We propose a general structural and thermodynamic model for self-assembly, in which a structural template controls assembly and shapes polymer formation into rings.
| Item Type: | Article |
|---|---|
| Subjects: | R Medicine > R Medicine (General) |
| Depositing User: | Repository Administrator |
| Date Deposited: | 14 Mar 2016 00:01 |
| Last Modified: | 17 Jan 2018 05:11 |
| URI: | https://eprints.victorchang.edu.au/id/eprint/388 |
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