2aka

From Proteopedia

Revision as of 06:03, 21 November 2007

Structure of the nucleotide-free myosin II motor domain from Dictyostelium discoideum fused to the GTPase domain of dynamin 1 from Rattus norvegicus

Overview

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.

About this Structure

2AKA is a Protein complex structure of sequences from Dictyostelium discoideum and Rattus norvegicus. Active as Dynamin GTPase, with EC number 3.6.5.5 Full crystallographic information is available from OCA.

Reference

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

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