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

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.

journal_name

Mol Biochem Parasitol

journal_title

Molecular and biochemical parasitology

authors

Barrack KL,Fyfe PK,Finney AJ,Hunter WN

doi

10.1016/j.molbiopara.2015.05.003

subject

Has Abstract

pub_date

2015-05-01 00:00:00

pages

26-30

issue

1

eissn

0166-6851

issn

1872-9428

pii

S0166-6851(15)30002-5

journal_volume

201

pub_type

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