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G domain dimerization controls dynamin's assembly-stimulated gtpase activity

Academic Article
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Overview

related to degree

  • Chappie, Joshua S, Ph.D. in Biology, Scripps Research 2003 - 2009

authors

  • Chappie, Joshua S
  • Acharya, S.
  • Leonard, M.
  • Schmid, Sandra
  • Dyda, F.

publication date

  • May 2010

journal

  • Nature  Journal

abstract

  • Dynamin is an atypical GTPase that catalyses membrane fission during clathrin-mediated endocytosis. The mechanisms of dynamin's basal and assembly-stimulated GTP hydrolysis are unknown, though both are indirectly influenced by the GTPase effector domain (GED). Here we present the 2.0 A resolution crystal structure of a human dynamin 1-derived minimal GTPase-GED fusion protein, which was dimeric in the presence of the transition state mimic GDP.AlF(4)(-).The structure reveals dynamin's catalytic machinery and explains how assembly-stimulated GTP hydrolysis is achieved through G domain dimerization. A sodium ion present in the active site suggests that dynamin uses a cation to compensate for the developing negative charge in the transition state in the absence of an arginine finger. Structural comparison to the rat dynamin G domain reveals key conformational changes that promote G domain dimerization and stimulated hydrolysis. The structure of the GTPase-GED fusion protein dimer provides insight into the mechanisms underlying dynamin-catalysed membrane fission.

subject areas

  • Aluminum Compounds
  • Amino Acid Sequence
  • Biocatalysis
  • Catalytic Domain
  • Conserved Sequence
  • Crystallography, X-Ray
  • Dynamin I
  • Enzyme Activation
  • Fluorides
  • GTP Phosphohydrolases
  • Guanosine Diphosphate
  • Humans
  • Hydrolysis
  • Models, Molecular
  • Protein Multimerization
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Sodium
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Identity

PubMed Central ID

  • PMC2879890

International Standard Serial Number (ISSN)

  • 0028-0836

Digital Object Identifier (DOI)

  • 10.1038/nature09032

PubMed ID

  • 20428113
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Additional Document Info

start page

  • 435

end page

  • 440

volume

  • 465

issue

  • 7297

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