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  RanGAP mediates GTP hydrolysis without an arginine finger

Seewald, M. J., Körner, C., Wittinghofer, A., & Vetter, I. R. (2002). RanGAP mediates GTP hydrolysis without an arginine finger. Nature <London>, 415(6872): 1, pp. 662-666. Retrieved from http://dx.doi.org/10.1038/415662a.

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Genre: Journal Article
Alternative Title : Nature

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 Creators:
Seewald, Michael J.1, Author
Körner, Carolin1, Author
Wittinghofer, Alfred2, Author           
Vetter, Ingrid R.3, Author           
Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753286              
2Sonstige Wissenschaftliche Organisationseinheiten, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753294              
3Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753287              

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 Abstract: GTPase-activating proteins (GAPs) increase the rate of GTP hydrolysis on guanine nucleotide-binding proteins by many orders of magnitude. Studies with Ras and Rho have elucidated the mechanism of GAP action by showing that their catalytic machinery is both stabilized by GAP binding and complemented by the insertion of a so-called 'arginine finger' into the phosphate-binding pocket(1,2). This has been proposed as a universal mechanism for GAP-mediated GTP hydrolysis. Ran is a nuclear Ras-related protein that regulates both transport between the nucleus and cytoplasm during interphase, and formation of the mitotic spindle and/or nuclear envelope in dividing cells(3). RanGTP is hydrolysed by the combined action of Ran-binding proteins (RanBPs) and RanGAP(4). Here we present the three-dimensional structure of a Ran-RanBP1-RanGAP ternary complex in the ground state and in a transition-state mimic. The structure and biochemical experiments show that RanGAP does not act through an arginine finger, that the basic machinery for fast GTP hydrolysis is provided exclusively by Ran and that correct positioning of the catalytic glutamine is essential for catalysis.

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Language(s): eng - English
 Dates: 2002-02-07
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 12576
URI: http://dx.doi.org/10.1038/415662a
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Title: Nature <London>
  Alternative Title : Nature
Source Genre: Journal
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Pages: - Volume / Issue: 415 (6872) Sequence Number: 1 Start / End Page: 662 - 666 Identifier: -