5AJ8

Tubulin Binding Cofactor C from Leishmania major

Summary for 5AJ8

• Entry DOI: 10.2210/pdb5aj8/pdb
• Descriptor: TUBULIN BINDING COFACTOR C (2 entities in total)
• Functional Keywords: structural protein
• Biological source: LEISHMANIA MAJOR
• Total number of polymer chains: 2
• Total formula weight: 41313.48

Authors

Barrack, K.L.,Fyfe, P.K.,Finney, A.J.,Hunter, W.N. (deposition date: 2015-02-20, release date: 2015-04-15, Last modification date: 2015-08-26)

Primary citation

Barrack, K.L.,Fyfe, P.K.,Finney, A.J.,Hunter, W.N.
Crystal Structure of the C-Terminal Domain of Tubulin-Binding Cofactor C from Leishmania Major.
Mol.Biochem.Parasitol., 201:26-, 2015

PubMed 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.

PubMed: 25982270
DOI: 10.1016/J.MOLBIOPARA.2015.05.003

Experimental method

X-RAY DIFFRACTION (2.2 Å)