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  The dynamin A ring complex: molecular organization and nucleotide‐dependent conformational changes

Klockow, B., Tichelaar, W., Madden, D. R., Niemann, H. H., Akiba, T., Hirose, K., et al. (2002). The dynamin A ring complex: molecular organization and nucleotide‐dependent conformational changes. EMBO Journal, 21(3), 240-250. doi:10.1093/emboj/21.3.240.

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Genre: Journal Article
Alternative Title : The dynamin A ring complex: molecular organization and nucleotide‐dependent conformational changes

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EMBOJ_21_2002_240.pdf (Any fulltext), 489KB
 
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 Creators:
Klockow, Boris1, Author              
Tichelaar, Willem2, Author              
Madden, Dean R.3, Author              
Niemann, Hartmut H., Author
Akiba, Toshihiko, Author
Hirose, Keiko, Author
Manstein, Dietmar J.1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              
3Max Planck Research Group Ion Channel Structure (Dean R. Madden), Max Planck Institute for Medical Research, Max Planck Society, ou_1497725              

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Free keywords: conformational changes; protease inhibitor; protein assembly; ring complex
 Abstract: Here we show that Dictyostelium discoideum dynamin A is a fast GTPase, binds to negatively charged lipids, and self‐assembles into rings and helices in a nucleotide‐dependent manner, similar to human dynamin‐1. Chemical modification of two cysteine residues, positioned in the middle domain and GTPase effector domain (GED), leads to altered assembly properties and the stabilization of a highly regular ring complex. Single particle analysis of this dynamin A* ring complex led to a three‐dimensional map, which shows that the nucleotide‐free complex consists of two layers with 11‐fold symmetry. Our results reveal the molecular organization of the complex and indicate the importance of the middle domain and GED for the assembly of dynamin family proteins. Nucleotide‐dependent changes observed with the unmodified and modified protein support a mechanochemical action of dynamin, in which tightening and stretching of a helix contribute to membrane fission.

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Language(s): eng - English
 Dates: 2001-12-052001-06-262001-12-052002-02-012002-02-01
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: EMBO Journal
  Other : EMBO J.
Source Genre: Journal
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Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 21 (3) Sequence Number: - Start / End Page: 240 - 250 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061