TssA from Aeromonas hydrophila: expression, purification and crystallographic studies.
Acta Crystallogr F Struct Biol Commun
; 74(Pt 9): 578-582, 2018 Sep 01.
Article
em En
| MEDLINE
| ID: mdl-30198891
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).
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Assunto principal:
Proteínas de Bactérias
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Aeromonas hydrophila
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Sistemas de Secreção Tipo VI
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Proteínas de Membrana
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article