Academic Journal
Structural Determinants Underlying Photoprotection in the Photoactive Orange Carotenoid Protein of Cyanobacteria
العنوان: | Structural Determinants Underlying Photoprotection in the Photoactive Orange Carotenoid Protein of Cyanobacteria |
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المؤلفون: | Wilson, Adjele, Kinney, James N, Zwart, Petrus H, Punginelli, Claire, d'Haene, Sandrine, Perreau, Francois, Klein, Mickael G, Kirilovsky, Diana, Kerfeld, Cheryl A |
المساهمون: | Institut de Biologie et de Technologies de Saclay (IBITECS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, United States Department of Energy, Joint Genome Institute (JGI), Institut Jean-Pierre Bourgin (IJPB), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Department of Plant and Microbial Biology, Agence Nationale de la Recherche (Program CAROPROTECT), CNRS, Commissariat à l’Energie Atomique (Saclay, France), United States Department of Energy’s Office of Science, Biological and Environmental Research, University of California, Lawrence Berkeley National Laboratory DE-AC02– 05CH11231, Lawrence Livermore National Laboratory DE-AC52- 07NA27344, National Science Foundation MCB-085170 |
المصدر: | ISSN: 0021-9258. |
بيانات النشر: | HAL CCSD American Society for Biochemistry and Molecular Biology |
سنة النشر: | 2010 |
المجموعة: | Institut National de la Recherche Agronomique: ProdINRA |
مصطلحات موضوعية: | chlorophyll-binding protein, synechocystis sp pcc-6803, short hydrogen-bonds, blue-light, energy-dissipation, phycobilisome fluorescence, rhodobacter-sphaeroides, signal-transduction, maximum-likelihood, crystal-structures, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM] |
الوصف: | 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. |
نوع الوثيقة: | article in journal/newspaper |
اللغة: | English |
Relation: | info:eu-repo/semantics/altIdentifier/pmid/20368334; hal-01203915; https://hal.science/hal-01203915; https://hal.science/hal-01203915/document; https://hal.science/hal-01203915/file/2010_Wilson_Journal%20of%20Biological%20Chemistry_1.pdf; PRODINRA: 45777; PUBMED: 20368334; WOS: 000278453900030 |
DOI: | 10.1074/jbc.M110.115709 |
الاتاحة: | https://hal.science/hal-01203915 https://hal.science/hal-01203915/document https://hal.science/hal-01203915/file/2010_Wilson_Journal%20of%20Biological%20Chemistry_1.pdf https://doi.org/10.1074/jbc.M110.115709 |
Rights: | http://hal.archives-ouvertes.fr/licences/copyright/ ; info:eu-repo/semantics/OpenAccess |
رقم الانضمام: | edsbas.6BA1C1C8 |
قاعدة البيانات: | BASE |
DOI: | 10.1074/jbc.M110.115709 |
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