ジャーナル: Cell / 年: 2009 タイトル: Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving. 著者: Harry H Low / Carsten Sachse / Linda A Amos / Jan Löwe / 要旨: Proteins of the dynamin superfamily mediate membrane fission, fusion, and restructuring events by polymerizing upon lipid bilayers and forcing regions of high curvature. In this work, we show the ...Proteins of the dynamin superfamily mediate membrane fission, fusion, and restructuring events by polymerizing upon lipid bilayers and forcing regions of high curvature. In this work, we show the electron cryomicroscopy reconstruction of a bacterial dynamin-like protein (BDLP) helical filament decorating a lipid tube at approximately 11 A resolution. We fitted the BDLP crystal structure and produced a molecular model for the entire filament. The BDLP GTPase domain dimerizes and forms the tube surface, the GTPase effector domain (GED) mediates self-assembly, and the paddle region contacts the lipids and promotes curvature. Association of BDLP with GMPPNP and lipid induces radical, large-scale conformational changes affecting polymerization. Nucleotide hydrolysis seems therefore to be coupled to polymer disassembly and dissociation from lipid, rather than membrane restructuring. Observed structural similarities with rat dynamin 1 suggest that our results have broad implication for other dynamin family members.
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2008年12月18日
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2009年12月22日
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2011年5月8日
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2011年7月13日
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2019年10月23日
Group: Author supporting evidence / Data collection / Other カテゴリ: cell / em_image_scans / em_single_particle_entity Item: _cell.Z_PDB