Open AccessCrystallization and preliminary X‐ray diffraction anaylsis of the LOV1 domains of phototropin 1 and 2 from Arabidopsis thaliana
Author(s) -
Nakasako Masayoshi,
Hirata Michihiro,
Shimizu Nobutaka,
Hosokawa Shyuntaro,
Matsuoka Daisuke,
Oka Toshihiko,
Yamamoto Masaki,
Tokutomi Satoru
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108015534
Subject(s) - phototropin , phototropism , biology , arabidopsis thaliana , arabidopsis , crystallography , physics , blue light , optoelectronics , biochemistry , chemistry , gene , mutant
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 P 2 1 2 1 2 1 , with unit‐cell parameters a = 61.2, b = 64.9, c = 70.8 Å, and diffracted X‐rays to a resolution of 2.1 Å. The crystal of the LOV1 domain of phototropin 2 belonged to space group P 2 1 , with unit‐cell parameters a = 32.5, b = 66.5, c = 56.7 Å, β = 92.4°, and diffracted X‐rays to beyond 2.0 Å resolution. In both crystals, two LOV1 domains occupied the crystallographic asymmetric unit.