Dataset Information

Crystallization and preliminary X-ray diffraction analysis [correction of anaylsis] of the LOV1 domains of phototropin 1 and 2 from Arabidopsis thaliana.

ABSTRACT: Phototropin is a blue-light receptor protein in plants that is responsible for phototropic responses, stomata opening and photo-induced relocation of chloroplasts. Higher plants such as Arabidopsis thaliana have two isoforms of phototropin: phototropin 1 and phototropin 2. Both isoforms comprise a tandem pair of blue-light-absorbing light-oxygen-voltage domains named LOV1 and LOV2 in the N-terminal half and a serine/threonine kinase domain in the C-terminal half. The LOV1 domain is thought to function as a dimerization site. In the present study, recombinant LOV1 domains of A. thaliana phototropin 1 and phototropin 2 were crystallized. The crystal of the LOV1 domain of phototropin 1 belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 61.2, b = 64.9, c = 70.8 A, and diffracted X-rays to a resolution of 2.1 A. The crystal of the LOV1 domain of phototropin 2 belonged to space group P2(1), with unit-cell parameters a = 32.5, b = 66.5, c = 56.7 A, beta = 92.4 degrees , and diffracted X-rays to beyond 2.0 A resolution. In both crystals, two LOV1 domains occupied the crystallographic asymmetric unit.

SUBMITTER: Nakasako M

PROVIDER: S-EPMC2443956 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis [correction of anaylsis] of the LOV1 domains of phototropin 1 and 2 from Arabidopsis thaliana.

Nakasako Masayoshi M Hirata Michihiro M Shimizu Nobutaka N Hosokawa Shyuntaro S Matsuoka Daisuke D Oka Toshihiko T Yamamoto Masaki M Tokutomi Satoru S

Acta crystallographica. Section F, Structural biology and crystallization communications 20080611 Pt 7

Phototropin is a blue-light receptor protein in plants that is responsible for phototropic responses, stomata opening and photo-induced relocation of chloroplasts. Higher plants such as Arabidopsis thaliana have two isoforms of phototropin: phototropin 1 and phototropin 2. Both isoforms comprise a tandem pair of blue-light-absorbing light-oxygen-voltage domains named LOV1 and LOV2 in the N-terminal half and a serine/threonine kinase domain in the C-terminal half. The LOV1 domain is thought to fu ...[more]

PMID: 18607090

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Project description:The Toll/interleukin-1 receptor (TIR) domain is a protein-protein interaction domain that is found in both animal and plant immune receptors. The N-terminal TIR domain from the nucleotide-binding (NB)-leucine-rich repeat (LRR) class of plant disease-resistance (R) proteins has been shown to play an important role in defence signalling. Recently, the crystal structure of the TIR domain from flax R protein L6 was determined and this structure, combined with functional studies, demonstrated that TIR-domain homodimerization is a requirement for function of the R protein L6. To advance the molecular understanding of the function of TIR domains in R-protein signalling, the protein expression, purification, crystallization and X-ray diffraction analyses of the TIR domains of the Arabidopsis thaliana R proteins RPS4 (resistance to Pseudomonas syringae 4) and RRS1 (resistance to Ralstonia solanacearum 1) and the resistance-like protein SNC1 (suppressor of npr1-1, constitutive 1) are reported here. RPS4 and RRS1 function cooperatively as a dual resistance-protein system that prevents infection by three distinct pathogens. SNC1 is implicated in resistance pathways in Arabidopsis and is believed to be involved in transcriptional regulation through its interaction with the transcriptional corepressor TPR1 (Topless-related 1). The TIR domains of all three proteins have successfully been expressed and purified as soluble proteins in Escherichia coli. Plate-like crystals of the RPS4 TIR domain were obtained using PEG 3350 as a precipitant; they diffracted X-rays to 2.05 Å resolution, had the symmetry of space group P1 and analysis of the Matthews coefficient suggested that there were four molecules per asymmetric unit. Tetragonal crystals of the RRS1 TIR domain were obtained using ammonium sulfate as a precipitant; they diffracted X-rays to 1.75 Å resolution, had the symmetry of space group P4(1)2(1)2 or P4(3)2(1)2 and were most likely to contain one molecule per asymmetric unit. Crystals of the SNC1 TIR domain were obtained using PEG 3350 as a precipitant; they diffracted X-rays to 2.20 Å resolution and had the symmetry of space group P4(1)2(1)2 or P4(3)2(1)2, with two molecules predicted per asymmetric unit. These results provide a good foundation to advance the molecular and structural understanding of the function of the TIR domain in plant innate immunity.

Dataset Information

Crystallization and preliminary X-ray diffraction analysis [correction of anaylsis] of the LOV1 domains of phototropin 1 and 2 from Arabidopsis thaliana.

Publications

Crystallization and preliminary X-ray diffraction analysis [correction of anaylsis] of the LOV1 domains of phototropin 1 and 2 from Arabidopsis thaliana.

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