2KOI
Refined solution structure of a cyanobacterial phytochrome GAF domain in the red light-absorbing ground state
Summary for 2KOI
| Entry DOI | 10.2210/pdb2koi/pdb |
| Descriptor | Sensor protein, PHYCOCYANOBILIN (2 entities in total) |
| Functional Keywords | phytochrome, gaf domain, phycocyanobilin, pcb, bacteriophytochrome, cyanobacterial phytochrome, kinase, phosphoprotein, transferase, protein structure initiative, psi-2, center for eukaryotic structural genomics, cesg, structural genomics |
| Biological source | Synechococcus sp. |
| Total number of polymer chains | 1 |
| Total formula weight | 19660.47 |
| Authors | Cornilescu, C.C.,Cornilescu, G.,Ulijasz, A.T.,Vierstra, R.D.,Markley, J.L.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2009-09-22, release date: 2009-11-03, Last modification date: 2024-11-06) |
| Primary citation | Ulijasz, A.T.,Cornilescu, G.,Cornilescu, C.C.,Zhang, J.,Rivera, M.,Markley, J.L.,Vierstra, R.D. Structural basis for the photoconversion of a phytochrome to the activated Pfr form Nature, 463:250-254, 2010 Cited by PubMed Abstract: Phytochromes are a collection of bilin-containing photoreceptors that regulate numerous photoresponses in plants and microorganisms through their ability to photointerconvert between a red-light-absorbing, ground state (Pr) and a far-red-light-absorbing, photoactivated state (Pfr). Although the structures of several phytochromes as Pr have been determined, little is known about the structure of Pfr and how it initiates signalling. Here we describe the three-dimensional solution structure of the bilin-binding domain as Pfr, using the cyanobacterial phytochrome from Synechococcus OSB'. Contrary to predictions, light-induced rotation of the A pyrrole ring but not the D ring is the primary motion of the chromophore during photoconversion. Subsequent rearrangements within the protein then affect intradomain and interdomain contact sites within the phytochrome dimer. On the basis of our models, we propose that phytochromes act by propagating reversible light-driven conformational changes in the bilin to altered contacts between the adjacent output domains, which in most phytochromes direct differential phosphotransfer. PubMed: 20075921DOI: 10.1038/nature08671 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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