Crystal structure of the GTPase domain of rat dynamin 1.
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.
Reubold
Thomas F
TF
Abteilung Biophysik, Max-Planck-Institut für Medizinische Forschung, Jahnstrasse 29, D-69120 Heidelberg, Germany.
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
D000818:Animals; D001120:Arginine; D002384:Catalysis; D003460:Crystallization; D018360:Crystallography, X-Ray; D034284:Dynamin I / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004789:Enzyme Activation / Q000235:genetics; D020558:GTP Phosphohydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D007700:Kinetics; D009154:Mutation; D017434:Protein Structure, Tertiary; D051381:Rats
D006160:Guanosine Triphosphate; D001120:Arginine; D034284:Dynamin I; D020558:GTP Phosphohydrolases