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

被引:117
作者
Prescott, M [1 ]
Ling, M
Beddoe, T
Oakley, AJ
Dove, S
Hoegh-Guldberg, O
Devenish, RJ
Rossjohn, J
机构
[1] Monash Univ, Sch Biomed Sci, Dept Biochem & Mol Biol, Clayton, Vic 3800, Australia
[2] Monash Univ, Sch Biomed Sci, Prot Crystallog Unit, Clayton, Vic 3800, Australia
[3] Univ Western Australia, Dept Pharmacol, Crystallog Ctr, Nedlands, WA 6009, Australia
[4] Univ Queensland, Ctr Marine Sci, St Lucia, Qld 4072, Australia
基金
英国惠康基金; 澳大利亚研究理事会;
关键词
pocilloporin; pigment; chromophore; fluorescence; green fluorescent protein; DsRed;
D O I
10.1016/S0969-2126(03)00028-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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, non-fluorescent pocilloporin to 2.2 Angstrom resolution and a genetically engineered fluorescent variant to 2.4 Angstrom resolution. The pocilloporin chromophore structure adopts a markedly different conformation in comparison with the DsRed chromophore, despite the chromophore sequences (Gin-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.
引用
收藏
页码:275 / 284
页数:10
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