Crystal structure of nucleotide-free dynamin

被引：239

作者：

Faelber, Katja ^{[1
]}

Posor, York ^{[2
]}

Gao, Song ^{[1
,2
]}

Held, Martin ^{[3
]}

Roske, Yvette ^{[1
]}

Schulze, Dennis ^{[1
]}

Haucke, Volker ^{[2
]}

Noe, Frank ^{[3
]}

Daumke, Oliver ^{[1
,4
]}

机构：

[1] Max Delbruck Ctr Mol Med, D-13125 Berlin, Germany

[2] Free Univ Berlin, Inst Chem & Biochem, D-14195 Berlin, Germany

[3] Free Univ Berlin, Inst Math, D-14195 Berlin, Germany

[4] Charite, Inst Med Phys & Biophys, D-10117 Berlin, Germany

来源：

NATURE | 2011年 / 477卷 / 7366期

关键词：

PLECKSTRIN HOMOLOGY DOMAIN; PARTICLE MESH EWALD; GTPASE DOMAIN; MIDDLE DOMAIN; PH DOMAIN; MODEL; PHOSPHORYLATION; IDENTIFICATION; RESOLUTION; MECHANISM;

D O I：

10.1038/nature10369

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Dynamin is a mechanochemical GTPase that oligomerizes around the neck of clathrin-coated pits and catalyses vesicle scission in a GTP-hydrolysis-dependent manner. The molecular details of oligomerization and the mechanism of the mechanochemical coupling are currently unknown. Here we present the crystal structure of human dynamin 1 in the nucleotide-free state with a four-domain architecture comprising the GTPase domain, the bundle signalling element, the stalk and the pleckstrin homology domain. Dynamin 1 oligomerized in the crystals via the stalks, which assemble in a criss-cross fashion. The stalks further interact via conserved surfaces with the pleckstrin homology domain and the bundle signalling element of the neighbouring dynamin molecule. This intricate domain interaction rationalizes a number of disease-related mutations in dynamin 2 and suggests a structural model for the mechanochemical coupling that reconciles previous models of dynamin function.

引用

页码：556 / U318

页数：7

共 59 条

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