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dc.contributor.author Horne, Christoper R.
dc.contributor.author Venugopal, Hariprasad
dc.contributor.author Panjikar, Santosh
dc.contributor.author Wood, David M.
dc.contributor.author Henrickson, Amy
dc.contributor.author Brookes, Emre
dc.contributor.author North, Rachel A.
dc.contributor.author Murphy, James M.
dc.contributor.author Friemann, Rosmarie
dc.contributor.author Griffin, Michael D. W.
dc.contributor.author Ramm, Georg
dc.contributor.author Demeler, Borries
dc.contributor.author Dobson, Renwick C. J.
dc.date.accessioned 2021-06-24T21:36:34Z
dc.date.available 2021-06-24T21:36:34Z
dc.date.issued 2021
dc.identifier.citation Horne, C. R., Venogopal, H., Panjikar, S., Wood, D. M., Henrickson, A., Brookes, E., North, R. A., Murphy, J. M., Friemann, R., Griffin, M. D., Ramm, G., Demeler, B., & Dobson, R. C. J. (2021). Mechanism of NanR gene repression and allosteric inducation of bacterial sialic acid metabolism. Nature Communications, 12, Article1988 (2021). https://doi.org/10.1038/s41467-021-22253-6 en_US
dc.identifier.uri https://hdl.handle.net/10133/5917
dc.description Open access article. Creative Commons Attribution 4.0 International License (CC BY 4.0) applies en_US
dc.description.abstract Bacteria respond to environmental changes by inducing transcription of some genes and repressing others. Sialic acids, which coat human cell surfaces, are a nutrient source for pathogenic and commensal bacteria. The Escherichia coli GntR-type transcriptional repressor, NanR, regulates sialic acid metabolism, but the mechanism is unclear. Here, we demonstrate that three NanR dimers bind a (GGTATA)3-repeat operator cooperatively and with high affinity. Single-particle cryo-electron microscopy structures reveal the DNA-binding domain is reorganized to engage DNA, while three dimers assemble in close proximity across the (GGTATA)3-repeat operator. Such an interaction allows cooperative protein-protein interactions between NanR dimers via their N-terminal extensions. The effector, N-acetylneuraminate, binds NanR and attenuates the NanR-DNA interaction. The crystal structure of NanR in complex with N-acetylneuraminate reveals a domain rearrangement upon N-acetylneuraminate binding to lock NanR in a conformation that weakens DNA binding. Our data provide a molecular basis for the regulation of bacterial sialic acid metabolism. en_US
dc.language.iso en_US en_US
dc.publisher Nature Publishing Group en_US
dc.subject Biophysical methods en_US
dc.subject Cryoelectron microscopy en_US
dc.subject Transcription en_US
dc.subject NanR
dc.subject Sialic acids
dc.subject DNA binding
dc.subject.lcsh DNA
dc.subject.lcsh X-ray crystallography
dc.title Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism en_US
dc.type Article en_US
dc.publisher.faculty Arts and Science en_US
dc.publisher.department Department of Chemistry and Biochemistry en_US
dc.description.peer-review Yes en_US
dc.publisher.institution University of Centerbury en_US
dc.publisher.institution Monash University en_US
dc.publisher.institution University of Lethbridge en_US
dc.publisher.institution University of Montana en_US
dc.publisher.institution University of Melbourne en_US
dc.publisher.institution Sahlgrenska University Hospital en_US
dc.publisher.institution University of Gothenburg en_US
dc.publisher.url https://doi.org/10.1038/s41467-021-22253-6 en_US


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