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

So Eun Kim, Kwang Yeon Hwang, Ki Hyun Nam

Research output: Contribution to journalArticle

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.

Original languageEnglish
JournalProtein Science
DOIs
Publication statusAccepted/In press - 2018 Jan 1

Fingerprint

Structural analysis
Spectrum analysis
Chromophores
Proteins
Hydrogen bonds
Biosensing Techniques
Hydrogen Bonding
Biosensors
Carrier concentration
Hydrogen
Salts
Crystal structure
Fluorescence
Metals
red fluorescent protein
Electrons

Keywords

  • Acropora digitifera
  • chromophore
  • decarboxylation
  • fluorescent protein
  • fluorescent protein
  • mutagenesis

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Spectral and structural analysis of a red fluorescent protein from Acropora digitifera. / Kim, So Eun; Hwang, Kwang Yeon; Nam, Ki Hyun.

In: Protein Science, 01.01.2018.

Research output: Contribution to journalArticle

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N2 - 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.

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