1ztu
From Proteopedia
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Structure of the chromophore binding domain of bacterial phytochrome
Overview
Phytochromes are red/far-red light photoreceptors that direct photosensory, responses across the bacterial, fungal and plant kingdoms. These include, photosynthetic potential and pigmentation in bacteria as well as, chloroplast development and photomorphogenesis in plants. Phytochromes, consist of an amino-terminal region that covalently binds a single bilin, chromophore, followed by a carboxy-terminal dimerization domain that often, transmits the light signal through a histidine kinase relay. Here we, describe the three-dimensional structure of the chromophore-binding domain, of Deinococcus radiodurans phytochrome assembled with its chromophore, biliverdin in the Pr ground state. Our model, refined to 2.5 A resolution, reaffirms Cys 24 as the chromophore attachment site, locates key amino, acids that form a solvent-shielded bilin-binding pocket, and reveals an, unusually formed deep trefoil knot that stabilizes this region. The, structure provides the first three-dimensional glimpse into the, photochromic behaviour of these photoreceptors and helps to explain the, evolution of higher plant phytochromes from prokaryotic precursors.
About this Structure
1ZTU is a Single protein structure of sequence from Deinococcus radiodurans with BLA as ligand. Full crystallographic information is available from OCA.
Reference
A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome., Wagner JR, Brunzelle JS, Forest KT, Vierstra RD, Nature. 2005 Nov 17;438(7066):325-31. PMID:16292304
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