PROSITE documentation PDOC51773
Orange 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.


Technical section

PROSITE method (with tools and information) covered by this documentation:

OCP_N, PS51773; Orange carotenoid protein (OCP) N-terminal domain profile  (MATRIX)


1AuthorsKerfeld C.A. Sawaya M.R. Brahmandam V. Cascio D. Ho K.K. Trevithick-Sutton C.C. Krogmann D.W. Yeates T.O.
TitleThe crystal structure of a cyanobacterial water-soluble carotenoid binding protein.
SourceStructure 11:55-65(2003).
PubMed ID12517340

2AuthorsWilson A. Kinney J.N. Zwart P.H. Punginelli C. D'Haene S. Perreau F. Klein M.G. Kirilovsky D. Kerfeld C.A.
TitleStructural determinants underlying photoprotection in the photoactive orange carotenoid protein of cyanobacteria.
SourceJ. Biol. Chem. 285:18364-18375(2010).
PubMed ID20368334

3AuthorsLeverenz R.L. Jallet D. Li M.-D. Mathies R.A. Kirilovsky D. Kerfeld C.A.
TitleStructural and functional modularity of the orange carotenoid protein: distinct roles for the N- and C-terminal domains in cyanobacterial photoprotection.
SourcePlant Cell 26:426-437(2014).
PubMed ID24399299

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