PROSITE documentation PDOC51773Orange carotenoid protein (OCP) N-terminal domain profile
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 serves as a sensor of light intensity and an effector of phycobilisome (PB)-associated photoprotection in cyanobacteria. Structurally, the OCP is composed of two distinct domains spanned by a single carotenoid chromophore. The OCP C-terminal is suggested to dynamically regulate the photoprotective activity on otherwise constitutively active carotenoid binding N-terminal domain [1,2,3].
The all-helical OCP N-terminal domain can be divided into two four-helix bundles (see <PDB:1M98>) [1,2,3].
The profile we developed covers the entire OCP N-terminal domain.
Last update:August 2015 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Kerfeld C.A. Sawaya M.R. Brahmandam V. Cascio D. Ho K.K. Trevithick-Sutton C.C. Krogmann D.W. Yeates T.O. |
| Title | The crystal structure of a cyanobacterial water-soluble carotenoid binding protein. | |
| Source | Structure 11:55-65(2003). | |
| PubMed ID | 12517340 |
| 2 | Authors | Wilson A. Kinney J.N. Zwart P.H. Punginelli C. D'Haene S. Perreau F. Klein M.G. Kirilovsky D. Kerfeld C.A. |
| Title | Structural determinants underlying photoprotection in the photoactive orange carotenoid protein of cyanobacteria. | |
| Source | J. Biol. Chem. 285:18364-18375(2010). | |
| PubMed ID | 20368334 | |
| DOI | 10.1074/jbc.M110.115709 |
| 3 | Authors | Leverenz R.L. Jallet D. Li M.-D. Mathies R.A. Kirilovsky D. Kerfeld C.A. |
| Title | Structural and functional modularity of the orange carotenoid protein: distinct roles for the N- and C-terminal domains in cyanobacterial photoprotection. | |
| Source | Plant Cell 26:426-437(2014). | |
| PubMed ID | 24399299 | |
| DOI | 10.1105/tpc.113.118588 |
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