Novel structure of an antikinase and its inhibitor

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dc.contributor.authorJacques, DAen_AU
dc.contributor.authorLangley, DBen_AU
dc.contributor.authorHynson, RMGen_AU
dc.contributor.authorWhitten, AEen_AU
dc.contributor.authorKwan, AHen_AU
dc.contributor.authorGuss, JMen_AU
dc.contributor.authorTrewhella, Jen_AU
dc.date.accessioned2011-03-08T00:45:32Zen_AU
dc.date.available2011-03-08T00:45:32Zen_AU
dc.date.issued2011-01-07en_AU
dc.date.statistics2011-01-07en_AU
dc.description.abstractIn Bacillus subtilis, the KipI protein is a regulator of the phosphorelay governing the onset of sporulation. KipI binds the relevant sensor histidine kinase, KinA, and inhibits the autophosphorylation reaction. Gene homologues of kipI are found almost ubiquitously throughout the bacterial kingdom and are usually located adjacent to, and often fused with, kipA gene homologues. In B. subtilis, the KipA protein inhibits the antikinase activity of KipI thereby permitting sporulation. We have used a combination of biophysical techniques in order to understand the domain structure and shape of the KipI–KipA complex and probe the nature of the interaction. We also have solved the crystal structure of TTHA0988, a Thermus thermophilus protein of unknown function that is homologous to a KipI–KipA fusion. This structure, which is the first to be described for this class of proteins, provides unique insight into the nature of the KipI–KipA complex. The structure confirms that KipI and KipA are proteins with two domains, and the C-terminal domains belong to the cyclophilin family. These cyclophilin domains are positioned in the complex such that their conserved surfaces face each other to form a large “bicyclophilin” cleft. We discuss the sequence conservation and possible roles across species of this near-ubiquitous protein family, which is poorly understood in terms of function. © 2011, Elsevier Ltd.en_AU
dc.identifier.citationJacques, D. A., Langley, D. B., Hynson, R. M. G., Whitten, A. E., Kwan, A., Guss, J. M., & Trewhella, J. (2011). Novel structure of an antikinase and its inhibitor. Journal of Molecular Biology, 405(1), 214-226. doi:10.1016/j.jmb.2010.10.047en_AU
dc.identifier.govdoc3281en_AU
dc.identifier.issn0022-2836en_AU
dc.identifier.issue1en_AU
dc.identifier.journaltitleJournal of Molecular Biologyen_AU
dc.identifier.pagination214-226en_AU
dc.identifier.urihttp://dx.doi.org/10.1016/j.jmb.2010.10.047en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/3123en_AU
dc.identifier.volume405en_AU
dc.language.isoenen_AU
dc.publisherElsevieren_AU
dc.subjectCrystal structureen_AU
dc.subjectPhosphotransferasesen_AU
dc.subjectHistidineen_AU
dc.subjectEnzyme inhibitorsen_AU
dc.subjectHydrolasesen_AU
dc.subjectProteinsen_AU
dc.titleNovel structure of an antikinase and its inhibitoren_AU
dc.typeJournal Articleen_AU
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