3SNH

Crystal structure of nucleotide-free human dynamin1

Summary for 3SNH

• Entry DOI: 10.2210/pdb3snh/pdb
• Descriptor: Dynamin-1 (1 entity in total)
• Functional Keywords: endocytosis, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q05193
• Total number of polymer chains: 1
• Total formula weight: 85071.15

Authors

Faelber, K.,Daumke, O. (deposition date: 2011-06-29, release date: 2011-09-21, Last modification date: 2023-09-13)

Primary citation

Faelber, K.,Posor, Y.,Gao, S.,Held, M.,Roske, Y.,Schulze, D.,Haucke, V.,Noe, F.,Daumke, O.
Crystal structure of nucleotide-free dynamin.
Nature, 477:556-560, 2011

PubMed 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.

PubMed: 21927000
DOI: 10.1038/nature10369

Experimental method

X-RAY DIFFRACTION (3.7 Å)