Crystal structure of the C-terminal domain of tubulin-binding cofactor C from Leishmania major.

摘要: Tubulin-binding cofactor C stimulates GTPase activity and contributes to the release of heterodimeric α/β-tubulin from a super-complex tubulin monomers two ancillary cofactors. We have determined 2.2 A resolution crystal structure C-terminal domain tubulin-binding Leishmania major based on single wavelength anomalous dispersion measurements targeting selenomethionine derivative. Although previously predicted consist domains is best described as dominated by right-handed β-helix five turns that form triangular prism. One face prism covered residues leaving another solvent exposed. Comparisons with an orthologous human activating protein match key involved in binding nucleotide identify fold likely interacting β-tubulin:GTP complex.