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Crystal structure of the GTPase domain of rat dynamin 1.

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.

SUBMITTER: Reubold TF

PROVIDER: S-EPMC1201622 | biostudies-literature | 2005 Sep

REPOSITORIES: biostudies-literature

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Crystal structure of the GTPase domain of rat dynamin 1.

Reubold Thomas F TF Eschenburg Susanne S Becker Andreas A Leonard Marilyn M Schmid Sandra L SL Vallee Richard B RB Kull F Jon FJ Manstein Dietmar J DJ

Proceedings of the National Academy of Sciences of the United States of America 20050902 37

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 ideall ...[more]

PMID: 16141317

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