1mou

From Proteopedia

Revision as of 19:28, 20 November 2007

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 with IOD as ligand. 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

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