Structure of the sporulation histidine kinase inhibitor Sda from bacillus subtilis and insights into its solution state

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dc.contributor.authorJacques, DAen_AU
dc.contributor.authorStreamer, Men_AU
dc.contributor.authorRowland, SLen_AU
dc.contributor.authorKing, GFen_AU
dc.contributor.authorGuss, JMen_AU
dc.contributor.authorTrewhella, Jen_AU
dc.contributor.authorLangley, DBen_AU
dc.date.accessioned2009-06-19T05:01:48Zen_AU
dc.date.accessioned2010-04-30T05:05:27Zen_AU
dc.date.available2009-06-19T05:01:48Zen_AU
dc.date.available2010-04-30T05:05:27Zen_AU
dc.date.issued2009-06en_AU
dc.date.statistics2009-06en_AU
dc.description.abstractThe crystal structure of the DNA-damage checkpoint inhibitor of sporulation, Sda, from Bacillus subtilis, has been solved by the MAD technique using selenomethionine-substituted protein. The structure closely resembles that previously solved by NMR, as well as the structure of a homologue from Geobacillus stearothermophilus solved in complex with the histidine kinase KinB. The structure contains three molecules in the asymmetric unit. The unusual trimeric arrangement, which lacks simple internal symmetry, appears to be preserved in solution based on an essentially ideal fit to previously acquired scattering data for Sda in solution. This interpretation contradicts previous findings that Sda was monomeric or dimeric in solution. This study demonstrates the difficulties that can be associated with the characterization of small proteins and the value of combining multiple biophysical techniques. It also emphasizes the importance of understanding the physical principles behind these techniques and therefore their limitations. © 2009, International Union of Crystallographyen_AU
dc.identifier.citationJacques, D. A., Streamer, M., Rowland, S. L., King, G. F., Guss, J. M., Trewhella, J., & Langley, D. B. (2009). Structure of the sporulation histidine kinase inhibitor Sda from bacillus subtilis and insights into its solution state. Acta Crystallographica Section D: Structural Biological, 65(6), 574-581. doi:10.1107/S090744490901169Xen_AU
dc.identifier.govdoc1353en_AU
dc.identifier.issn0907-4449en_AU
dc.identifier.issue6en_AU
dc.identifier.journaltitleActa Crystallographica Section D: Structural Biologicalen_AU
dc.identifier.pagination574-581en_AU
dc.identifier.urihttp://dx.doi.org/10.1107/S090744490901169Xen_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/1438en_AU
dc.identifier.volume65en_AU
dc.language.isoenen_AU
dc.publisherInternational Union of Crystallographyen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectCrystal structureen_AU
dc.subjectDNAen_AU
dc.subjectProteinsen_AU
dc.subjectNuclear magnetic resonanceen_AU
dc.subjectMoleculesen_AU
dc.titleStructure of the sporulation histidine kinase inhibitor Sda from bacillus subtilis and insights into its solution stateen_AU
dc.typeJournal Articleen_AU
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