1MOV

Crystal structure of Coral protein mutant

Summary for 1MOV

• Entry DOI: 10.2210/pdb1mov/pdb
• Related: 1MOU
• Descriptor: GFP-like non-fluorescent chromoprotein, IODIDE ION (3 entities in total)
• Functional Keywords: coral pigment, fluorescent conversion mutant, chromophore, rtms5, luminescent protein
• Biological source: Montipora efflorescens
• Total number of polymer chains: 1
• Total formula weight: 25398.58

Authors

Prescott, M.,Ling, M.,Beddoe, T.,Oakley, A.J.,Dove, S.,Hoegh-Guldberg, O.,Devenish, R.J.,Rossjohn, J. (deposition date: 2002-09-10, release date: 2003-04-08, Last modification date: 2024-11-06)

Primary citation

Prescott, M.,Ling, M.,Beddoe, T.,Oakley, A.J.,Dove, S.,Hoegh-Guldberg, O.,Devenish, R.J.,Rossjohn, J.
The 2.2 a crystal structure of a pocilloporin pigment reveals a nonplanar chromophore conformation.
Structure, 11:275-284, 2003

PubMed Abstract: 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.

PubMed: 12623015
DOI: 10.1016/S0969-2126(03)00028-5

Experimental method

X-RAY DIFFRACTION (2.4 Å)