1mou
From Proteopedia
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| , resolution 2.2Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Coral pigment
Overview
Reef-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.
About this Structure
1MOU is a Single protein structure of sequence from Montipora efflorescens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 12:46:12 2008
