Abstract:
: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.
journal_name
Naturejournal_title
Natureauthors
Faelber K,Posor Y,Gao S,Held M,Roske Y,Schulze D,Haucke V,Noé F,Daumke Odoi
10.1038/nature10369subject
Has Abstractpub_date
2011-09-18 00:00:00pages
556-60issue
7366eissn
0028-0836issn
1476-4687pii
nature10369journal_volume
477pub_type
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