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

doi:10.1107/S2053230X15000990

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 journal › Article › peer-review

4 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 language	English
Pages (from-to)	539-546
Number of pages	8
Journal	Acta Crystallographica Section F: Structural Biology Communications
Volume	71
Issue number	5
DOIs	https://doi.org/10.1107/S2053230X15000990
Publication status	Published - May 2015

Keywords

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

ASJC Scopus subject areas

Biochemistry
Biophysics
Genetics
Structural Biology
Condensed Matter Physics

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10.1107/S2053230X15000990

Cite this

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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",

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.",

keywords = "Chaperone, Helical fold, Molecular parasitology - advances in biology and supporting drug discovery, Protein-protein interactions, Selenomethionine, Tubulin-binding protein",

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language = "English",

volume = "71",

pages = "539--546",

journal = "Acta Crystallographica Section F: Structural Biology Communications",

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publisher = "International Union of Crystallography",

number = "5",

}

The structure of tubulin-binding cofactor A from Leishmania major infers a mode of association during the early stages of microtubule assembly. / Barrack, Keri L.; Fyfe, Paul K.; Hunter, William N. (Lead / Corresponding author).
In: Acta Crystallographica Section F: Structural Biology Communications, Vol. 71, No. 5, 05.2015, p. 539-546.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - The structure of tubulin-binding cofactor A from Leishmania major infers a mode of association during the early stages of microtubule assembly

AU - Barrack, Keri L.

AU - Fyfe, Paul K.

AU - Hunter, William N.

PY - 2015/5

Y1 - 2015/5

N2 - 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.

AB - 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.

KW - Chaperone

KW - Helical fold

KW - Molecular parasitology - advances in biology and supporting drug discovery

KW - Protein-protein interactions

KW - Selenomethionine

KW - Tubulin-binding protein

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DO - 10.1107/S2053230X15000990

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SN - 2053-230X

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IS - 5

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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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

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State-of-the-Art Facilities for Structural Biology at the University of Dundee

Aref#d: 19401. Structure, specificity and mechanism of biosynthetic enzymes in trypanosomatids and inhibitor discovery of essential microbial functions (Programme Grant)

Cite this

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Projects

State-of-the-Art Facilities for Structural Biology at the University of Dundee

Aref#d: 19401. Structure, specificity and mechanism of biosynthetic enzymes in trypanosomatids and inhibitor discovery of essential microbial functions (Programme Grant)

Cite this