Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/79246
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dc.contributor.authorPendini, N.en
dc.contributor.authorYap, M.en
dc.contributor.authorPolyak, S.en
dc.contributor.authorCowieson, N.en
dc.contributor.authorAbell, A.en
dc.contributor.authorBooker, G.en
dc.contributor.authorWallace, J.en
dc.contributor.authorWilce, J.en
dc.contributor.authorWilce, M.en
dc.date.issued2013en
dc.identifier.citationProtein Science, 2013; 22(6):762-773en
dc.identifier.issn0961-8368en
dc.identifier.issn1469-896Xen
dc.identifier.urihttp://hdl.handle.net/2440/79246-
dc.descriptionCorrected by: Erratum: Structural characterisation of Staphylococcus aureus biotin protein ligase and interaction partners: An antibiotic target, in Vol. 23, Issue 1, 121. Daouda Traore, was inadvertently omitted from the published version of their manuscript.en
dc.description.abstractThe essential metabolic enzyme biotin protein ligase (BPL) is a potential target for the development of new antibiotics required to combat drug-resistant pathogens. Staphylococcus aureus BPL (SaBPL) is a bifunctional protein, possessing both biotin ligase and transcription repressor activities. This positions BPL as a key regulator of several important metabolic pathways. Here, we report the structural analysis of both holo- and apo-forms of SaBPL using X-ray crystallography. We also present small-angle X-ray scattering data of SaBPL in complex with its biotin-carboxyl carrier protein substrate as well as the SaBPL:DNA complex that underlies repression. This has revealed the molecular basis of ligand (biotinyl-5'-AMP) binding and conformational changes associated with catalysis and repressor function. These data provide new information to better understand the bifunctional activities of SaBPL and to inform future strategies for antibiotic discovery.en
dc.description.statementofresponsibilityNicole R. Pendini, Min Y. Yap, Steven W. Polyak, Nathan P. Cowieson, Andrew Abell, Grant W. Booker, John C. Wallace, Jacqueline A. Wilce, and Matthew C. J. Wilceen
dc.language.isoenen
dc.publisherCold Spring Harbor Lab Pressen
dc.rights© 2013 The Protein Societyen
dc.subjectbiotin protein ligase; biotin-carboxyl carrier protein; DNA-binding; bacterial enzyme; biotinylation; small-angle X-ray scatteringen
dc.titleStructural characterization of Staphylococcus aureus biotin protein ligase and interaction partners: An antibiotic targeten
dc.typeJournal articleen
dc.identifier.rmid0020130273en
dc.identifier.doi10.1002/pro.2262en
dc.identifier.pubid18984-
pubs.library.collectionMolecular and Biomedical Science publicationsen
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
dc.identifier.orcidPolyak, S. [0000-0002-8458-5194]en
dc.identifier.orcidAbell, A. [0000-0002-0604-2629]en
dc.identifier.orcidBooker, G. [0000-0001-7207-4699]en
Appears in Collections:Molecular and Biomedical Science publications

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