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3MG2

Crystal structure of the orange carotenoid protein Y44S mutant from cyanobacteria synechocystis sp. PCC 6803

Replaces:  3I1W
Summary for 3MG2
Entry DOI10.2210/pdb3mg2/pdb
Related1M98 3MG1 3MG3
DescriptorOrange carotenoid protein, beta,beta-caroten-4-one (3 entities in total)
Functional Keywordscarotenoid binding protein, echinone, phycobilisome
Biological sourceSynechocystis sp.
Total number of polymer chains2
Total formula weight71860.34
Authors
Wilson, A.,Kinney, J.,Zwart, P.H.,Punginelli, C.,D'Haen, S.,Perreau, F.,Klein, M.G.,Kirilovsky, D.,Kerfeld, C.A. (deposition date: 2010-04-05, release date: 2010-04-14, Last modification date: 2023-09-06)
Primary citationWilson, A.,Kinney, J.N.,Zwart, P.H.,Punginelli, C.,D'Haene, S.,Perreau, F.,Klein, M.G.,Kirilovsky, D.,Kerfeld, C.A.
Structural determinants underlying photoprotection in the photoactive orange carotenoid protein of cyanobacteria.
J.Biol.Chem., 285:18364-18375, 2010
Cited by
PubMed Abstract: The photoprotective processes of photosynthetic organisms involve the dissipation of excess absorbed light energy as heat. Photoprotection in cyanobacteria is mechanistically distinct from that in plants; it involves the orange carotenoid protein (OCP), a water-soluble protein containing a single carotenoid. The OCP is a new member of the family of blue light-photoactive proteins; blue-green light triggers the OCP-mediated photoprotective response. Here we report structural and functional characterization of the wild type and two mutant forms of the OCP, from the model organism Synechocystis PCC6803. The structural analysis provides high resolution detail of the carotenoid-protein interactions that underlie the optical properties of the OCP, unique among carotenoid-proteins in binding a single pigment per polypeptide chain. Collectively, these data implicate several key amino acids in the function of the OCP and reveal that the photoconversion and photoprotective responses of the OCP to blue-green light can be decoupled.
PubMed: 20368334
DOI: 10.1074/jbc.M110.115709
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.653 Å)
Structure validation

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