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          Institute: MPI für medizinische Forschung     Collection: Max-Planck-Forschungsgruppe Ionenkanalstruktur (Dean R. Madden)     Display Documents

ID: 23076.0, MPI für medizinische Forschung / Max-Planck-Forschungsgruppe Ionenkanalstruktur (Dean R. Madden)
The dynamin A ring complex: molecular organisation and nucleotide-dependent conformational changes
Translation of Title:The dynamin A ring complex: molecular organisation and nucleotide-dependent conformational changes
Authors:Klockow, Boris; Tichelaar, Willem; Madden, Dean R.; Niemann, Hartmut H.; Akiba, Toshihiko; Hirose, Keiko; Manstein, Dietmar J.
Date of Publication (YYYY-MM-DD):2002
Title of Journal:EMBO Journal
Journal Abbrev.:EMBO J.
Issue / Number:3
Start Page:240
End Page:250
Copyright:© European Molecular Biology Organization
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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.
Free Keywords:conformational changes; protease inhibitor; protein assembly; ring complex
Comment of the Author/Creator:We thank Helga Clasen for expert technical assistance, Marin van Heel for helpful advice with single particle analysis, B.Brügger and F.T.Wieland for help and advice with liposome preparation and lipid interaction assays, A.Schlosser and W.Lehmann for mass spectrometry, F.Jon Kull for stimulating discussion and Kenneth C.Holmes for support. The Boehringer Ingelheim Fonds supported B.K. and H.H.N.
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
MPI für medizinische Forschung/Nachwuchsgruppe Ion Channel Structure
External Affiliations:Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA; National Institute for Advanced Interdisciplinary Research; Gene Discovery Research Center, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-4 Higashi, Tsukuba, Ibaraki 305-8562, Japan
Identifiers:URI:http://emboj.oupjournals.org/cgi/content/full/21/3... [Fulltext HTML]
URI:http://emboj.oupjournals.org/cgi/content/abstract/... [Abstract]
URI:http://emboj.oupjournals.org/cgi/reprint/21/3/240 [Fulltext PDF]
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