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Crystallization and preliminary X-ray studies of the chromophore-binding domain of cyanobacteriochrome AnPixJ from Anabaena sp. PCC 7120.


ABSTRACT: Cyanobacteriochromes form a recently defined superfamily of tetrapyrrole-based photoreceptors that are distantly related to conventional red/far-red photoreceptor phytochromes. Among these molecules, AnPixJ from Anabaena sp. PCC 7120 is a novel photoreceptor that shows reversible photoconversion between green-absorbing and red-absorbing forms, which is in contrast to the properties of conventional phytochromes. In order to better understand the structural basis of this unique photoconversion mechanism, the chromophore-binding domain of AnPixJ (AnPixJ-GAF2) was heterologously overproduced and purified, and crystallization of both forms was attempted. Blue crystals of the red-absorbing form of AnPixJ-GAF2 were successfully obtained; they belonged to space group P4(3)2(1)2 and contained one monomer per asymmetric unit. Diffraction data were collected to a resolution of 1.8 A using synchrotron-radiation beamline BL-5A at the Photon Factory.

SUBMITTER: Narikawa R 

PROVIDER: S-EPMC2635879 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray studies of the chromophore-binding domain of cyanobacteriochrome AnPixJ from Anabaena sp. PCC 7120.

Narikawa Rei R   Muraki Norifumi N   Shiba Tomoo T   Ikeuchi Masahiko M   Kurisu Genji G  

Acta crystallographica. Section F, Structural biology and crystallization communications 20090131 Pt 2


Cyanobacteriochromes form a recently defined superfamily of tetrapyrrole-based photoreceptors that are distantly related to conventional red/far-red photoreceptor phytochromes. Among these molecules, AnPixJ from Anabaena sp. PCC 7120 is a novel photoreceptor that shows reversible photoconversion between green-absorbing and red-absorbing forms, which is in contrast to the properties of conventional phytochromes. In order to better understand the structural basis of this unique photoconversion mec  ...[more]

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