Crystal structure of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana

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Authors	KLUMPLER Tomáš PEKÁROVÁ Blanka MAREK Jaromír BORKOVCOVÁ Pavla JANDA Lubomír HEJÁTKO Jan
Year of publication	2009
Type	Conference abstract
MU Faculty or unit	Faculty of Science
Citation
Description	The crystal structure of the receiver domain (RD) of the histidine kinase CYTOKININ-INDEPENDENT1 (CKI1) from Arabidopsis thaliana has been determined at a resolution of 2.0 Angstroem. Crystals of the recombinant RD of CKI1 have been obtained. The crystals diffracted at beamline BW7B of the DORIS-III storage ring to approx. 2.4 Angstroem.The crystals belong to space group C2221 with unit-cell parameters a=54.46, b=99.82, c=79.94 Angstroem, the asymmetric unit contains one molecule of the protein. The structure of CKI1RD had been solved by a molecular-replacement. Initial R value of 0.54, which decreased to R = 0.413 and Rfree = 0.426 after 30 cycles of REFMAC refinement. The three-dimensional structure of A. thaliana CKI1RD shows the conformational conservation of receiver proteins, such as CheY, CheB, ETRRD. CKI1RD is a single domain protein folded in a Rossmann manner with a central beta-sheet formed from five beta-strands and surrounded by sides by two and three alpha-helices.
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