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Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms

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Scherer,  Anna
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Manstein,  Dietmar J.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Kull,  F. Jon
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Niemann, H. H., Knetsch, M. L. W., Scherer, A., Manstein, D. J., & Kull, F. J. (2001). Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms. The EMBO Journal, 21(21), 5813-5821. doi:10.1093/emboj/20.21.5813.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0028-FD70-3
Abstract
Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating function has been suggested for dynamins. Here we report the 2.3 Å crystal structure of the nucleotide-free and GDP-bound GTPase domain of Dictyostelium discoideum dynamin A. The GTPase domain is the most highly conserved region among dynamins. The globular structure contains the G-protein core fold, which is extended from a six-stranded β-sheet to an eight-stranded one by a 55 amino acid insertion. This topologically unique insertion distinguishes dynamins from other subfamilies of GTP-binding proteins. An additional N-terminal helix interacts with the C-terminal helix of the GTPase domain, forming a hydrophobic groove, which could be occupied by C-terminal parts of dynamin not present in our construct. The lack of major conformational changes between the nucleotide-free and the GDP-bound state suggests that mechanochemical rearrangements in dynamin occur during GTP binding, GTP hydrolysis or phosphate release and are not linked to loss of GDP.