Hughes, Adam Michael, Wilson, Samuel, Dodson, Eleanor J. et al. (2 more authors) (2019) Crystal structure of the putative peptide-binding protein AppA from Clostridium difficile. Acta Crystallographica Section F:Structural Biology Communications. pp. 246-253. ISSN 2053-230X
Abstract
Peptides play an important signalling role in Bacillus subtilis, where their uptake by one of two ABC-type oligopeptide transporters, Opp and App, is required for efficient sporulation. Homologues of these transporters in Clostridium difficile have been characterized, but their role, and hence that of peptides, in regulating sporulation in this organism is less clear. Here, the oligopeptide-binding receptor proteins for these transporters, CdAppA and CdOppA, have been purified and partially characterized, and the crystal structure of CdAppA has been determined in an open unliganded form. Peptide binding to either protein could not be observed in Thermofluor assays with a set of ten peptides of varying lengths and compositions. Re-examination of the protein sequences together with structure comparisons prompts the proposal that CdAppA is not a versatile peptide-binding protein but instead may bind a restricted set of peptides. Meanwhile, CdOppA is likely to be the receptor protein for a nickel-uptake system.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2019 International Union of Crystallography. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 30 Jul 2019 14:30 |
Last Modified: | 16 Oct 2024 15:53 |
Published Version: | https://doi.org/10.1107/S2053230X1900178X |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1107/S2053230X1900178X |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:149125 |