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

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.

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Genre: Journal Article
Alternative Title : Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms

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EMBOJ_20_2001_5813.pdf (Any fulltext), 402KB
 
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 Creators:
Niemann, Hartmut H., Author
Knetsch, Menno L. W., Author
Scherer, Anna1, Author              
Manstein, Dietmar J.2, Author              
Kull, F. Jon2, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: crystal structure; Dictyostelium discoideum; dynamin; GTPase
 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.

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Language(s): eng - English
 Dates: 2001-09-112001-08-102001-09-132001-11-012001-11-01
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: The EMBO Journal
Source Genre: Journal
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Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 21 (21) Sequence Number: - Start / End Page: 5813 - 5821 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061_1