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ABSTRACT Tubulin-binding cofactor C stimulates GTPase activity and contributes to the release of the heterodimeric α/β-tubulin from a super-complex of tubulin monomers and two ancillary cofactors. We have determined the 2.2 Å resolution crystal structure of the C-terminal domain of tubulin-binding cofactor C from Leishmania major based on single wavelength anomalous dispersion measurements targeting a selenomethionine derivative. Although previously predicted to consist of two domains the structure is best described as a single domain dominated by a right-handed β-helix of five turns that form a triangular prism. One face of the prism is covered by the C-terminal residues leaving another face solvent exposed. Comparisons with an orthologous human GTPase activating protein match key residues involved in binding nucleotide and identify the face of the β-helix fold likely involved in interacting with the β-tubulin:GTP complex.
- Abbreviations ARL3 ADPribosylation factor-like protein 3
- CARP cyclase-associated proteins and X-linked retinitis pigmentosa 2 gene products
- LmTBCC TBCC from Leishmania major
- LmTBCC-C C-terminal domain of the L. major protein
- NMR nuclear magnetic resonance spectroscopy
- PDB protein data bank
- PEG 2000 MME polyethylene glycol monomethyl ether
- RP2 retinitis pigmentosa 2 protein
- SAD single-wavelength anomalous dispersion
- SeMet selenomethionine
- TBC tubulin-binding cofactor
- TEV tobacco etch virus
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