Document Type

Article

Publication Date

2005

Publication Title

Proceedings of the National Academy of Sciences of the United States of America

Department

Department of Chemistry

Abstract

Here, we present the 1.9-A crystal structure of the nucleotide-free GTPase domain of dynamin 1 from Rattus norvegicus. The structure corresponds to an extended form of the canonical GTPase fold observed in Ras proteins. Both nucleotide-binding switch motifs are well resolved, adopting conformations that closely resemble a GTP-bound state not previously observed for nucleotide-free GTPases. Two highly conserved arginines, Arg-66 and Arg-67, greatly restrict the mobility of switch I and are ideally positioned to relay information about the nucleotide state to other parts of the protein. Our results support a model in which switch I residue Arg-59 gates GTP binding in an assembly-dependent manner and the GTPase effector domain functions as an assembly-dependent GTPase activating protein in the fashion of RGS-type GAPs.

DOI

10.1073/pnas.0506491102

Original Citation

Reubold TF, Eschenburg S, Becker A, Leonard M, Schmid SL, Vallee RB, Kull FJ, Manstein DJ. Crystal structure of the GTPase domain of rat dynamin 1. Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13093-8. doi: 10.1073/pnas.0506491102. Epub 2005 Sep 2. PMID: 16141317; PMCID: PMC1201622.

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