Structure of a Bacterial Dynamin-like Protein Lipid Tube Provides a Mechanism For Assembly and Membrane Curving

被引：146

作者：

Low, Harry H. ^{[1
]}

Sachse, Carsten ^{[1
]}

Amos, Linda A. ^{[1
]}

Lowe, Jan ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 0QH, England

来源：

CELL | 2009年 / 139卷 / 07期

基金：

英国生物技术与生命科学研究理事会;

关键词：

CRYSTAL-STRUCTURE; MITOCHONDRIAL FUSION; BINDING PROTEINS; GTPASE DOMAIN; CONSTRICTION; RESOLUTION; MODEL; CONFORMATION; CYTOSKELETON; INSTABILITY;

D O I：

10.1016/j.cell.2009.11.003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 similar to 11 angstrom 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.

引用

页码：1342 / 1352

页数：11

共 42 条

[1] GTPase Cycle of Dynamin Is Coupled to Membrane Squeeze and Release, Leading to Spontaneous Fission [J].