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

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

    Research output: Contribution to journalArticle

    3 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)539-546
    Number of pages8
    JournalActa Crystallographica Section F: Structural Biology Communications
    Volume71
    Issue number5
    DOIs
    Publication statusPublished - May 2015

    Keywords

    • Chaperone
    • Helical fold
    • Molecular parasitology - advances in biology and supporting drug discovery
    • Protein-protein interactions
    • Selenomethionine
    • Tubulin-binding protein

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