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

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Publikace nespadá pod Filozofickou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.
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KLUMPLER Tomáš PEKÁROVÁ Blanka MAREK Jaromír BORKOVCOVÁ Pavla JANDA Lubomír HEJÁTKO Jan

Rok publikování 2009
Druh Konferenční abstrakty
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
Popis 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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