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From Proteopedia
Crystal structure of Coral protein mutant
Structural highlights
FunctionNFCP_MONEF Thought to play a role in photoprotection of the coral's resident symbiont microalgae's photosystems from photoinhibition caused by high light levels found near the surface of coral reefs.[1] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedReef-building corals contain host pigments, termed pocilloporins, that function to regulate the light environment of their resident microalgae by acting as a photoprotectant in excessive sunlight. We have determined the crystal structure of an intensely blue, nonfluorescent pocilloporin to 2.2 A resolution and a genetically engineered fluorescent variant to 2.4 A resolution. The pocilloporin chromophore structure adopts a markedly different conformation in comparison with the DsRed chromophore, despite the chromophore sequences (Gln-Tyr-Gly) being identical; the tyrosine ring of the pocilloporin chromophore is noncoplanar and in the trans configuration. Furthermore, the fluorescent variant adopted a noncoplanar chromophore conformation. The data presented here demonstrates that the conformation of the chromophore is highly dependent on its immediate environment. The 2.2 A crystal structure of a pocilloporin pigment reveals a nonplanar chromophore conformation.,Prescott M, Ling M, Beddoe T, Oakley AJ, Dove S, Hoegh-Guldberg O, Devenish RJ, Rossjohn J Structure. 2003 Mar;11(3):275-84. PMID:12623015[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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