The 2.2 A crystal structure of a pocilloporin pigment reveals a nonplanar chromophore conformation

Structure. 2003 Mar;11(3):275-84. doi: 10.1016/s0969-2126(03)00028-5.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anthozoa / chemistry*
  • Crystallography, X-Ray
  • Green Fluorescent Proteins
  • Luminescent Proteins / genetics
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Pigments, Biological / chemistry*
  • Pigments, Biological / genetics
  • Protein Conformation
  • Red Fluorescent Protein

Substances

  • Luminescent Proteins
  • Pigments, Biological
  • Green Fluorescent Proteins

Associated data

  • PDB/1MOU
  • PDB/1MOV