2AKA

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

Summary for 2AKA

• Entry DOI: 10.2210/pdb2aka/pdb
• Descriptor: myosin II heavy chain, LINKER, Dynamin-1, ... (4 entities in total)
• Functional Keywords: fusion protein, gtpase domain, dynamin, myosin, contractile protein
• Biological source: Dictyostelium discoideum; More
• Cellular location: Cytoplasm, cell cortex: P08799; Cytoplasm. Isoform 2: Cytoplasm. Isoform 6: Cytoplasm: P21575
• Total number of polymer chains: 3
• Total formula weight: 123253.81

Authors

Reubold, T.F.,Eschenburg, S.,Becker, A.,Leonard, M.,Schmid, S.L.,Vallee, R.B.,Kull, F.J.,Manstein, D.J. (deposition date: 2005-08-03, release date: 2005-08-23, Last modification date: 2024-10-30)

Primary citation

Reubold, T.F.,Eschenburg, S.,Becker, A.,Leonard, M.,Schmid, S.L.,Vallee, R.B.,Kull, F.J.,Manstein, D.J.
Crystal structure of the GTPase domain of rat dynamin 1.
Proc.Natl.Acad.Sci.Usa, 102:13093-13098, 2005

PubMed 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.

PubMed: 16141317
DOI: 10.1073/pnas.0506491102

Experimental method

X-RAY DIFFRACTION (1.9 Å)