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The structure of tubulin‐binding cofactor A from Leishmania major infers a mode of association during the early stages of microtubule assembly
Author(s) -
Barrack Keri L.,
Fyfe Paul K.,
Hunter William N.
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15000990
Subject(s) - microtubule , tubulin , biology , biogenesis , microbiology and biotechnology , computational biology , biochemistry , chemistry , gene
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.