Edmonds, Katherine A, Zhang, Yifan, Raines, Daniel J orcid.org/0000-0002-3015-6327 et al. (2 more authors) (2020) 1H, 13C, 15N backbone resonance assignments of the apo and holo forms of the ABC transporter solute binding protein PiuA from Streptococcus pneumoniae. Biomolecular NMR Assignments. ISSN 1874-270X
Abstract
Streptococcus pneumoniae is a Gram-positive human pathogen that causes millions of infections worldwide with an increasing occurrence of antibiotic resistance. Iron acquisition is essential for its survival and virulence, especially under host-imposed nutritional immunity. S. pneumoniae expresses several ATP-binding cassette (ABC) transporters to facilitate acquisition under iron limitation, including PitABCD, PiaABCD, and PiuBCDA. The substrate specificity of PiuBCDA is not fully established. Herein, we report the backbone 1H, 13C and 15N resonance assignments of the 31 kDa soluble, extracellular domain of the substrate binding protein PiuA in the apo form and in complex with Ga(III) and the catechol siderophore-mimic 4-LICAM. These studies provide valuable information for further functional studies of interactions with other proteins, metals, and small molecules.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2020 Springer Nature Switzerland AG. Part of Springer Nature. This is an author-produced version of the published paper. 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) |
Funding Information: | Funder Grant number EPSRC EP/L024829/1 UNSPECIFIED EP/T007338/1 |
Depositing User: | Pure (York) |
Date Deposited: | 11 Aug 2020 15:50 |
Last Modified: | 22 Dec 2024 00:14 |
Published Version: | https://doi.org/10.1007/s12104-020-09952-9 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1007/s12104-020-09952-9 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:164250 |
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