Crystal structure of CKI1 receiver domain from Arabidopsis

KLUMPLER, Tomáš, Blanka PEKÁROVÁ, Jaromir MAREK, Lubomír JANDA and Jan HEJÁTKO. Crystal structure of CKI1 receiver domain from Arabidopsis. In 7th International Conference of Ph.D Students on Experimental Plant Biology "News - what the plants told us". Brno. 2009. ISBN 978-80-7375-310-8.

Basic information

• Original name: Crystal structure of CKI1 receiver domain from Arabidopsis
• Authors: KLUMPLER, Tomáš (203 Czech Republic, guarantor), Blanka PEKÁROVÁ (203 Czech Republic), Jaromir MAREK (203 Czech Republic), Lubomír JANDA (203 Czech Republic) and Jan HEJÁTKO (203 Czech Republic).
• Edition: 7th International Conference of Ph.D Students on Experimental Plant Biology "News - what the plants told us". Brno, 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/00216224:14310/09:00039825
• Organization unit: Faculty of Science
• ISBN: 978-80-7375-310-8
• Keywords in English: Arabidopsis cytokinin signaling CKI1 crystallography crystal structure

Abstract

Sensor histidine kinases (HKs) are members of the two-component (TC) signalling systems that mediate signal transduction in a broad spectrum of adaptive responses in bacteria. The sensor histidine kinase CKI1 was identified as an activator of a cytokinin-like response when overexpressed in hypocotyl explants of A. thaliana. However, in contrast to the genuine cytokinin receptors of A. thaliana, AHK2, AHK3 and AHK4, CKI1 was found to be constitutively active in bacteria and yeast or A. thaliana protoplasts. Thus, the specificity and the role of CKI1 in the TC signalling in A. thaliana remain unclear. The three-dimensional structure of A. thaliana CKI1RD was determined. The catalytic aspartate residue is located on the carboxyl terminus of the central beta3-strand, in a cavity formed by loops L1, L5 and L7 loops. All major conformational differences between receiver proteins are located in the loops, which supposedly form a docking interface for the ineracting partners.

Links

• LC06034, research and development project: Name: 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