Structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition

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dc.contributor.authorWhitten, AEen_AU
dc.contributor.authorJacques, DAen_AU
dc.contributor.authorHammouda, Ben_AU
dc.contributor.authorHanley, TLen_AU
dc.contributor.authorKing, GFen_AU
dc.contributor.authorGuss, JMen_AU
dc.contributor.authorTrewhella, Jen_AU
dc.contributor.authorLangley, DBen_AU
dc.date.accessioned2008-04-23T02:34:39Zen_AU
dc.date.accessioned2010-04-30T05:01:39Zen_AU
dc.date.available2008-04-23T02:34:39Zen_AU
dc.date.available2010-04-30T05:01:39Zen_AU
dc.date.issued2007-04-27en_AU
dc.date.statistics2007-04en_AU
dc.description.abstractThe Bacillus subtilis histidine kinase KinA controls activation of the transcription factor governing sporulation, SpoOA. The decision to sporulate involves KinA phosphorylating itself on a conserved histidine residue, after which the phosphate moiety is relayed via two other proteins to SpoOA. The DNA-damage checkpoint inhibitor Sda halts this pathway by binding KinA and blocking the autokinase reaction. We have performed small-angle X-ray scattering and neutron contrast variation studies on the complex formed by KinA and Sda. The data show that two Sda molecules bind to the base of the DHp dimerization domain of the KinA dimer. In this position Sda does riot appear to be able to sterically block the catalytic domain from accessing its target histidine, as previously proposed, but rather may effect an allosteric mode of inhibition involving transmission of the inhibitory signal via the four-helix bundle that forms the DHp domain. © 2007, Elsevier Ltd.en_AU
dc.identifier.citationWhitten, A. E., Jacques, D. A., Hammouda, B., Hanley, T., King, G. F., Guss, J. M., et al. (2007). The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. Journal of Molecular Biology, 368(2), 407-420. doi:10.1016/j.jmb.2007.01.064en_AU
dc.identifier.govdoc1096en_AU
dc.identifier.issn0022-2836en_AU
dc.identifier.issue2en_AU
dc.identifier.journaltitleJournal of Molecular Biologyen_AU
dc.identifier.pagination407-420en_AU
dc.identifier.urihttp://dx.doi.org/10.1016/j.jmb.2007.01.064en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/1108en_AU
dc.identifier.volume368en_AU
dc.language.isoenen_AU
dc.publisherElsevieren_AU
dc.subjectPhosphotransferasesen_AU
dc.subjectHistidineen_AU
dc.subjectInhibitionen_AU
dc.subjectProteinsen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectDNAen_AU
dc.titleStructure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibitionen_AU
dc.typeJournal Articleen_AU
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