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PMID: 21927000 Published · epublish English Journal Article Research Support, Non-U.S. Gov't

Crystal structure of nucleotide-free dynamin.

Nature ·Vol. 477 ·No. 7366 ·2011-09-18 ·Pages 556-60

Faelber K, Posor Y, Gao S, Held M, Roske Y, Schulze D, Haucke V, Noé F, Daumke O

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.

MeSH Terms
Crystallography, X-Ray Dynamin I/chemistry,metabolism Dynamin II/genetics,metabolism GTP Phosphohydrolases/chemistry,metabolism Guanosine Triphosphate/metabolism HeLa Cells Humans Hydrolysis Models, Molecular Molecular Dynamics Simulation Nucleotides Protein Binding Protein Structure, Tertiary Signal Transduction Transferrin/metabolism
Chemicals
Nucleotides Transferrin Guanosine Triphosphate Dynamin I GTP Phosphohydrolases Dynamin II
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Faelber Katja
Crystallography, Max-Delbrück-Centrum for Molecular Medicine, Robert-Rössle-Strasse 10, 13125 Berlin, Germany. [email protected]
Posor York
Gao Song
Held Martin
Roske Yvette
Schulze Dennis
Haucke Volker
Noé Frank
Daumke Oliver
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Article Info
Journal
Nature
Abbr.
Nature
ISSN
1476-4687
Published
2011-09-18
Epub
2011-00-18
Pages
556-60
Language
English
Region
England
NLM ID
0410462
Subset
IM
Databases
PDB
Analysis Services
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