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

Keri L. Barrack, Paul K. Fyfe, Alex J. Finney, William N. Hunter (Lead / Corresponding author)

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3 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)26-30
Number of pages5
JournalMolecular and Biochemical Parasitology
Volume201
Issue number1
DOIs
Publication statusPublished - May 2015

Keywords

  • 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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