Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/82176
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dc.contributor.authorCounago, R.en
dc.contributor.authorWeen, M.en
dc.contributor.authorBegg, S.en
dc.contributor.authorBajaj, M.en
dc.contributor.authorZuegg, J.en
dc.contributor.authorO'Mara, M.en
dc.contributor.authorCooper, M.en
dc.contributor.authorMcEwan, A.en
dc.contributor.authorPaton, J.en
dc.contributor.authorKobe, B.en
dc.contributor.authorMcDevitt, C.en
dc.date.issued2014en
dc.identifier.citationNature Chemical Biology, 2014; 10(1):35-43en
dc.identifier.issn1552-4450en
dc.identifier.issn1552-4469en
dc.identifier.urihttp://hdl.handle.net/2440/82176-
dc.description.abstractThe relative stability of divalent first-row transition metal ion complexes, as defined by the Irving-Williams series, poses a fundamental chemical challenge for selectivity in bacterial metal ion acquisition. Here we show that although the substrate-binding protein of Streptococcus pneumoniae, PsaA, is finely attuned to bind its physiological substrate manganese, it can also bind a broad range of other divalent transition metal cations. By combining high-resolution structural data, metal-binding assays and mutational analyses, we show that the inability of open-state PsaA to satisfy the preferred coordination chemistry of manganese enables the protein to undergo the conformational changes required for cargo release to the Psa permease. This is specific for manganese ions, whereas zinc ions remain bound to PsaA. Collectively, these findings suggest a new ligand binding and release mechanism for PsaA and related substrate-binding proteins that facilitate specificity for divalent cations during competition from zinc ions, which are more abundant in biological systems.en
dc.description.statementofresponsibilityRafael M Couñago, Miranda P Ween, Stephanie L Begg, Megha Bajaj, Johannes Zuegg, Megan L O’Mara, Matthew A Cooper, Alastair G McEwan, James C Paton, Bostjan Kobe, & Christopher A McDevitten
dc.language.isoenen
dc.publisherNature Publishing Groupen
dc.rights© 2014 Nature America, Inc. All rights reserved.en
dc.subjectStreptococcus pneumoniae; Cations; Metals; Membrane Transport Proteins; Binding Sites; Models, Molecularen
dc.titleImperfect coordination chemistry facilitates metal ion release in the Psa permeaseen
dc.typeJournal articleen
dc.identifier.rmid0020134403en
dc.identifier.doi10.1038/NCHEMBIO.1382en
dc.identifier.pubid16544-
pubs.library.collectionMolecular and Biomedical Science publicationsen
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
Appears in Collections:Molecular and Biomedical Science publications

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