Tubulin-binding cofactor A (TBCA) participates in microtubule formation, a key process in eukaryotic biology to create the cytoskeleton. There is little information on how TBCA might interact with β-tubulin en route to microtubule biogenesis. To address this, the protozoan Leishmania major was targeted as a model system. The crystal structure of TBCA and comparisons with three orthologous proteins are presented. The presence of conserved features infers that electrostatic interactions that are likely to involve the C-terminal tail of β-tubulin are key to association. This study provides a reagent and template to support further work in this area.
|Number of pages||8|
|Journal||Acta Crystallographica Section F: Structural Biology Communications|
|Publication status||Published - May 2015|
- Helical fold
- Molecular parasitology - advances in biology and supporting drug discovery
- Protein-protein interactions
- Tubulin-binding protein