Structural highlights
Function
[PHEA_MASLA] Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Phycobiliproteins and phytochromes are light-harvesting and light-sensing proteins containing linear tetrapyrroles, so-called bile chromophores. The chromophores in certain biliproteins, including the phytochromes, isomerize reversibly from a stable Z-configuration to a stable E-configuration when irradiated with light of the appropriate wavelength. Here, we report the crystal structure of alpha-phycoerythrocyanin with its chromophore in the E-configuration, compare it with the Z-configuration found in trimeric phycoerythrocyanin, and reveal the structural bases of the isomerization. The geometric changes of the chromophore account for the large spectral shift, which characterizes the overall transition. Interactions of the chromophore A and D pyrrole rings with flexible protein moieties are required for the formation and stabilization of the isomers. We predict that the results will hold for all photoactive biliproteins.
Structural basis for the photochemistry of alpha-phycoerythrocyanin.,Schmidt M, Patel A, Zhao Y, Reuter W Biochemistry. 2007 Jan 16;46(2):416-23. PMID:17209552[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schmidt M, Patel A, Zhao Y, Reuter W. Structural basis for the photochemistry of alpha-phycoerythrocyanin. Biochemistry. 2007 Jan 16;46(2):416-23. PMID:17209552 doi:10.1021/bi061844j
