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Protein Sci. 2019 Feb;28(2):375-381. doi: 10.1002/pro.3540. Epub 2018 Nov 27.

Spectral and structural analysis of a red fluorescent protein from Acropora digitifera.

Author information

1
Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul, 02841, Republic of Korea.
2
Institute of Life Science and Natural Resources, Korea University, Seoul, 02841, Republic of Korea.

Abstract

Fluorescent proteins (FPs) possess a wide variety of spectral properties that make them of widespread interest as optical markers. These proteins can be applied as pH indicators or metal biosensors. The discovery and characterization of new fluorescent proteins is expected to further extend their application. Here, we report the spectral and structural analysis of a red fluorescent protein from Acropora digitifera (designated AdRed). This protein shows a tetrameric state and is red emitting, with excitation and emission maxima at 567 and 612 nm, respectively. Its crystal structure shows the tetrameric interface stabilized by hydrogen bonding and salt bridges. The electron density map of the chromophore, consisting of Asp66-Tyr67-Gly68, shows the decarboxylated side chain of Asp66. Ser223, located near the chromophore, has the role of bridging His202 and Glu221, and is part of the hydrogen bond network. Mutated AdRed with Cys148Ser reveals a blue shift in fluorescence excitation and emission. Our results provide insights into understanding the molecular function of AdRed and other FPs.

KEYWORDS:

Acropora digitifera; chromophore; decarboxylation; fluorescent protein; mutagenesis

PMID:
30368951
PMCID:
PMC6319757
[Available on 2020-02-01]
DOI:
10.1002/pro.3540

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