TssA from Aeromonas hydrophila: Expression, purification and crystallographic studies

Samuel R. Dix; Ruyue Sun; Matthew J. Harris; Sarah L. Batters; Svetlana E. Sedelnikova; Patrick J. Baker; Mark S. Thomas; David W. Rice

doi:10.1107/S2053230X18010439

TssA from Aeromonas hydrophila: Expression, purification and crystallographic studies

Samuel R. Dix
, Ruyue Sun
, Matthew J. Harris
, Sarah L. Batters
, Svetlana E. Sedelnikova
, Patrick J. Baker
, Mark S. Thomas
, David W. Rice^*

^*Corresponding author for this work

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

1 Citation (Scopus)

Abstract

TssA is a core subunit of the type VI secretion system, which is a major player in interspecies competition in Gram-negative bacteria. Previous studies on enteroaggregative Escherichia coli TssA suggested that it is comprised of three putative domains: a conserved N-terminal domain, a middle domain and a ringforming C-terminal domain. X-ray studies of the latter two domains have identified their respective structures. Here, the results of the expression and purification of full-length and domain constructs of TssA from Aeromonas hydrophila are reported, resulting in diffraction-quality crystals for the middle domain (Nt2) and a construct including the middle and C-terminal domains (Nt2-CTD).

Original language	English
Pages (from-to)	578-582
Number of pages	5
Journal	Acta Crystallographica Section F: Structural Biology Communications
Volume	74
Issue number	9
DOIs	https://doi.org/10.1107/S2053230X18010439
Publication status	Published - Sept 2018

Keywords

Aeromonas hydrophila
TssA subunit
Type VI secretion system

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10.1107/S2053230X18010439

Cite this

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title = "TssA from Aeromonas hydrophila: Expression, purification and crystallographic studies",

abstract = "TssA is a core subunit of the type VI secretion system, which is a major player in interspecies competition in Gram-negative bacteria. Previous studies on enteroaggregative Escherichia coli TssA suggested that it is comprised of three putative domains: a conserved N-terminal domain, a middle domain and a ringforming C-terminal domain. X-ray studies of the latter two domains have identified their respective structures. Here, the results of the expression and purification of full-length and domain constructs of TssA from Aeromonas hydrophila are reported, resulting in diffraction-quality crystals for the middle domain (Nt2) and a construct including the middle and C-terminal domains (Nt2-CTD).",

keywords = "Aeromonas hydrophila, TssA subunit, Type VI secretion system",

author = "Dix, \{Samuel R.\} and Ruyue Sun and Harris, \{Matthew J.\} and Batters, \{Sarah L.\} and Sedelnikova, \{Svetlana E.\} and Baker, \{Patrick J.\} and Thomas, \{Mark S.\} and Rice, \{David W.\}",

year = "2018",

month = sep,

doi = "10.1107/S2053230X18010439",

language = "English",

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pages = "578--582",

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

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TY - JOUR

T1 - TssA from Aeromonas hydrophila

T2 - Expression, purification and crystallographic studies

AU - Dix, Samuel R.

AU - Sun, Ruyue

AU - Harris, Matthew J.

AU - Batters, Sarah L.

AU - Sedelnikova, Svetlana E.

AU - Baker, Patrick J.

AU - Thomas, Mark S.

AU - Rice, David W.

PY - 2018/9

Y1 - 2018/9

N2 - TssA is a core subunit of the type VI secretion system, which is a major player in interspecies competition in Gram-negative bacteria. Previous studies on enteroaggregative Escherichia coli TssA suggested that it is comprised of three putative domains: a conserved N-terminal domain, a middle domain and a ringforming C-terminal domain. X-ray studies of the latter two domains have identified their respective structures. Here, the results of the expression and purification of full-length and domain constructs of TssA from Aeromonas hydrophila are reported, resulting in diffraction-quality crystals for the middle domain (Nt2) and a construct including the middle and C-terminal domains (Nt2-CTD).

AB - TssA is a core subunit of the type VI secretion system, which is a major player in interspecies competition in Gram-negative bacteria. Previous studies on enteroaggregative Escherichia coli TssA suggested that it is comprised of three putative domains: a conserved N-terminal domain, a middle domain and a ringforming C-terminal domain. X-ray studies of the latter two domains have identified their respective structures. Here, the results of the expression and purification of full-length and domain constructs of TssA from Aeromonas hydrophila are reported, resulting in diffraction-quality crystals for the middle domain (Nt2) and a construct including the middle and C-terminal domains (Nt2-CTD).

KW - Aeromonas hydrophila

KW - TssA subunit

KW - Type VI secretion system

UR - https://www.scopus.com/pages/publications/85053129261

U2 - 10.1107/S2053230X18010439

DO - 10.1107/S2053230X18010439

M3 - Article

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AN - SCOPUS:85053129261

SN - 2053-230X

VL - 74

SP - 578

EP - 582

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

IS - 9

ER -

TssA from Aeromonas hydrophila: Expression, purification and crystallographic studies

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Keywords

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