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TssA from Aeromonas hydrophila : expression, purification and crystallographic studies
Author(s) -
Dix Samuel R.,
Sun Ruyue,
Harris Matthew J.,
Batters Sarah L.,
Sedelnikova Svetlana E.,
Baker Patrick J.,
Thomas Mark S.,
Rice David W.
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18010439
Subject(s) - aeromonas hydrophila , escherichia coli , biology , protein subunit , domain (mathematical analysis) , bacteria , computational biology , microbiology and biotechnology , gene , genetics , mathematical analysis , mathematics
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).