KLUMPLER, Tomáš, Blanka PEKÁROVÁ, Jaromír MAREK, Pavla BORKOVCOVÁ, Lubomír JANDA and Jan HEJÁTKO. Crystal structure of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana. In Kolokvium - Struktura 2009. 2009. ISSN 1211-5894.
Other formats:   BibTeX LaTeX RIS
Basic information
Original name Crystal structure of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana
Authors KLUMPLER, Tomáš (203 Czech Republic, guarantor), Blanka PEKÁROVÁ (203 Czech Republic), Jaromír MAREK (203 Czech Republic), Pavla BORKOVCOVÁ (203 Czech Republic), Lubomír JANDA (203 Czech Republic) and Jan HEJÁTKO (203 Czech Republic).
Edition Kolokvium - Struktura 2009, 2009.
Other information
Original language English
Type of outcome Conference abstract
Field of Study Genetics and molecular biology
Country of publisher Czech Republic
Confidentiality degree is not subject to a state or trade secret
RIV identification code RIV/00216224:14310/09:00039824
Organization unit Faculty of Science
ISSN 1211-5894
Keywords in English histidinkinase CKI1 Arabidopsis cytokinin signaling crystal structure
Changed by Changed by: Mgr. Tomáš Klumpler, Ph.D., učo 55204. Changed: 31/3/2010 10:51.
Abstract
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.
Links
LC06034, research and development projectName: Regulace morfogeneze rostlinných buněk a orgánů
Investor: Ministry of Education, Youth and Sports of the CR, Regulation of morphogenesis of plant cells and organs
MSM0021622415, plan (intention)Name: Molekulární podstata buněčných a tkáňových regulací
Investor: Ministry of Education, Youth and Sports of the CR, Molecular basis of cell and tissue regulations
PrintDisplayed: 23/8/2024 20:23