Proceedings of the National Academy of Sciences of the United States of America
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.
Dartmouth Digital Commons Citation
Reubold, Thomas F.; Eschenburg, Susanne; Becker, Andreas; Leonard, Marilyn; Schmid, Sandra L.; Vallee, Richard B.; Kull, F. Jon; and Manstein, Dietmar J., "Crystal Structure of the GTPase Domain of Rat Dynamin 1" (2005). Open Dartmouth: Peer-reviewed articles by Dartmouth faculty. 1386.