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PDBsum entry 3snh
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References listed in PDB file
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Key reference
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Title
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Crystal structure of nucleotide-Free dynamin.
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Authors
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K.Faelber,
Y.Posor,
S.Gao,
M.Held,
Y.Roske,
D.Schulze,
V.Haucke,
F.Noé,
O.Daumke.
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Ref.
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Nature, 2011,
477,
556-560.
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PubMed id
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Abstract
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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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