A 12 Å carotenoid translocation in a photoswitch associated with cyanobacterial photoprotection

Author:

Leverenz Ryan L.1,Sutter Markus12,Wilson Adjélé34,Gupta Sayan5,Thurotte Adrien34,Bourcier de Carbon Céline34,Petzold Christopher J.2,Ralston Corie5,Perreau François6,Kirilovsky Diana34,Kerfeld Cheryl A.127

Affiliation:

1. MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI 48824, USA.

2. Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

3. Commissariat à l’Energie Atomique (CEA), Institut de Biologie et Technologies de Saclay (iBiTec-S), 91191 Gif-sur-Yvette, France.

4. Centre National de la Recherche Scientifique (CNRS), I2BC, UMR 9198, 91191 Gif-sur-Yvette, France.

5. Berkeley Center for Structural Biology, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

6. INRA, Institut Jean-Pierre Bourgin, UMR 1318, ERL CNRS 3559, Saclay Plant Sciences, RD10, F-78026 Versailles, France.

7. Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA.

Abstract

Protection from too much light Photosynthetic organisms protect themselves from too much light using pigment photoswitches that absorb excess energy. Leverenz et al. analyzed the structure of an active, energy-dissipating form of the orange carotenoid protein (OCP) from a cyanobacterium. When activated by excess light, OCP moves its hydrophobic carotenoid pigment 12 Å within the protein to accommodate nonphotochemical quenching by the broader photosynthetic antenna complex. Science , this issue p. 1463

Funder

Howard Hughes Medical Institute

U.S. Department of Energy

National Institute of General Medical Sciences

Basic Energy Sciences

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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