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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 ring-forming 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).

SUBMITTER: Dix SR

PROVIDER: S-EPMC6130423 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature

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TssA from Aeromonas hydrophila: expression, purification and crystallographic studies.

Dix Samuel R SR Sun Ruyue R Harris Matthew J MJ Batters Sarah L SL Sedelnikova Svetlana E SE Baker Patrick J PJ Thomas Mark S MS Rice David W DW

Acta crystallographica. Section F, Structural biology communications 20180903 Pt 9

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 ring-forming 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 domai ...[more]

PMID: 30198891

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