Crystal Structure of the GTPase Domain of Rat Dynamin 1

Here, we present the 1.9-Å 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...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 102; no. 37; pp. 13093 - 13098
Main Authors Reubold, Thomas F., Eschenburg, Susanne, Becker, Andreas, Leonard, Marilyn, Schmid, Sandra L., Vallee, Richard B., Kull, F. Jon, Manstein, Dietmar J., Taylor, Edwin W.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 13.09.2005
National Acad Sciences
Subjects
Animals
Arginine
Atoms
Biological Sciences
Biophysics
Catalysis
Crystal structure
Crystallization
Crystallography, X-Ray
Crystals
Dynamin I - chemistry
Dynamin I - genetics
Dynamin I - metabolism
Enzyme Activation - genetics
Enzymes
Genetic mutation
GTP Phosphohydrolases - chemistry
GTP Phosphohydrolases - genetics
GTP Phosphohydrolases - metabolism
GTPase activating proteins
Guanosine Triphosphate - metabolism
Hydrolysis
Kinetics
Lipids
Molecules
Mutation
Nucleotides
Protein Structure, Tertiary
Proteins
Rats
Rattus norvegicus
Rodents
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Summary:Here, we present the 1.9-Å 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.
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Present address: Department of Medicinal Chemistry, University of Kansas, 4038 Malott Hall, Lawrence, KS 66045.
Abbreviations: GAP, GTPase-activating protein; GED, GTPase effector domain.
Author contributions: T.F.R., S.L.S., F.J.K., R.B.V., and D.J.M. designed research; T.F.R., S.E., A.B., M.L., F.J.K., and D.J.M. performed research; A.B., S.L.S., R.B.V., and D.J.M. contributed new reagents/analytic tools; T.F.R., S.E., M.L., S.L.S., F.J.K., and D.J.M. analyzed data; and T.F.R., S.E., S.L.S., and D.J.M. wrote the paper.
Data deposition: The atomic coordinates and structure factors have been deposited in the Protein Data Bank, www.pdb.org (PDB ID code 2AKA).
Present address: Abteilung Strukturelle Biologie, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Communicated by Edwin W. Taylor, Northwestern University, Chicago, IL, August 1, 2005
To whom correspondence should be addressed. E-mail: manstein@bpc.mh-hannover.de.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0506491102