The structure of tubulin-binding cofactor A from Leishmania major infers a mode of association during the early stages of microtubule assembly

Journal Article · Tue Apr 21 04:00:00 EDT 2015 · Acta crystallographica. Section F, Structural biology communications

DOI:https://doi.org/10.1107/S2053230X15000990· OSTI ID:22375719

Barrack, Keri L.; Fyfe, Paul K.

The structure of a tubulin-binding cofactor from L. major is reported and compared with yeast, plant and human orthologues. 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.

• OSTI ID: 22375719
• Journal Information: Acta crystallographica. Section F, Structural biology communications, Journal Name: Acta crystallographica. Section F, Structural biology communications Journal Issue: Pt 5 Vol. 71; ISSN ACSFEN; ISSN 2053-230X
• Country of Publication: United States
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTAL STRUCTURE
INTERACTIONS
MICROTUBULES
PROTEINS