4CQI

Crystal structure of recombinant tubulin-binding cofactor A (TBCA) from Leishmania major

Summary for 4CQI

• Entry DOI: 10.2210/pdb4cqi/pdb
• Descriptor: TUBULIN-BINDING COFACTOR A, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: structural protein, tubulin-binding cofactor a
• Biological source: LEISHMANIA MAJOR
• Total number of polymer chains: 1
• Total formula weight: 14413.10

Authors

Barrack, K.L.,Fyfe, P.K.,Hunter, W.N. (deposition date: 2014-02-17, release date: 2014-11-26, Last modification date: 2024-10-16)

Primary citation

Barrack, K.L.,Fyfe, P.K.,Hunter, W.N.
The Structure of Tubulin-Binding Cofactor a from Leishmania Major Infers a Mode of Association During the Early Stages of Microtubule Assembly
Acta Crystallogr.,Sect.F, 71:539-, 2015

PubMed 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.

PubMed: 25945706
DOI: 10.1107/S2053230X15000990

Experimental method

X-RAY DIFFRACTION (1.9 Å)