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

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.
Authors:
; ;  [1]
  1. University of Dundee, Dow Street, Dundee DD1 5EH, Scotland (United Kingdom)
Publication Date:
OSTI Identifier:
22375719
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta crystallographica. Section F, Structural biology communications; Journal Volume: 71; Journal Issue: Pt 5; Other Information: PMCID: PMC4427162; PMID: 25945706; PUBLISHER-ID: tb5074; PUBLISHER-ID: S2053230X15000990; OAI: oai:pubmedcentral.nih.gov:4427162; Copyright (c) Barrack et al. 2015; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTAL STRUCTURE; INTERACTIONS; MICROTUBULES; PROTEINS