期刊
NATURE
卷 477, 期 7366, 页码 556-U318出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nature10369
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资金
- Deutsche Forschungsgemeinschaft [SFB 740/C7, SFB958/A12, SFB740/D7, SFB958/A04, SFB740/C8, SFB 958/A7]
- International Human Frontier Science Program Organization
- EMBO
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.
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