Dix, S.R., Sun, R., Harris, M.J. et al. (5 more authors) (2018) TssA from Aeromonas hydrophila: expression, purification and crystallographic studies. Acta Crystallographica Section F: Structural Biology Communications, 74. pp. 578-582. ISSN 2053-230X
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).
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2018 International Union of Crystallography. Reproduced in accordance with the publisher's self-archiving policy. |
Keywords: | type VI secretion system; TssA subunit; Aeromonas hydrophila |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) The University of Sheffield > Sheffield Teaching Hospitals |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 12 Oct 2018 09:14 |
Last Modified: | 12 Oct 2018 15:58 |
Published Version: | https://doi.org/10.1107/S2053230X18010439 |
Status: | Published |
Publisher: | International Union of Crystallography |
Refereed: | Yes |
Identification Number: | 10.1107/S2053230X18010439 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:137027 |