Crystal structures of Dronpa complexed with quenchable metal ions provide insight into metal biosensor development

In Jung Kim; Sangsoo Kim; Jeahyun Park; Intae Eom; Sunam Kim; Jin Hong Kim; Sung Chul Ha; Yeon Gil Kim; Kwang Yeon Hwang; Ki Hyun Nam

doi:10.1002/1873-3468.12316

Crystal structures of Dronpa complexed with quenchable metal ions provide insight into metal biosensor development

In Jung Kim, Sangsoo Kim, Jeahyun Park, Intae Eom, Sunam Kim, Jin Hong Kim, Sung Chul Ha, Yeon Gil Kim, Kwang Yeon Hwang, Ki Hyun Nam

Division of Biotechnology

Research output: Contribution to journal › Letter › peer-review

11 Citations (Scopus)

Abstract

Many fluorescent proteins (FPs) show fluorescence quenching by specific metal ions, which can be applied towards metal biosensor development. In this study, we investigated the significant fluorescence quenching of Dronpa by Co²⁺ and Cu²⁺ ions. Crystal structures of Co²⁺-, Ni²⁺- and Cu²⁺ -bound Dronpa revealed previously unseen, unique, metal-binding sites for fluorescence quenching. These metal ions commonly interact with surface-exposed histidine residues (His194-His210 and His210-His212), and interact indirectly with chromophores. Structural analysis of the Co²⁺- and Cu²⁺- binding sites of Dronpa provides insight into FP-based metal biosensor engineering.

Original language	English
Pages (from-to)	2982-2990
Number of pages	9
Journal	FEBS Letters
DOIs	https://doi.org/10.1002/1873-3468.12316
Publication status	Published - 2016 Sept 1

Keywords

biosensor
Dronpa
fluorescent protein
metal-binding site
quenching

ASJC Scopus subject areas

Structural Biology
Biophysics
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1002/1873-3468.12316

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title = "Crystal structures of Dronpa complexed with quenchable metal ions provide insight into metal biosensor development",

abstract = "Many fluorescent proteins (FPs) show fluorescence quenching by specific metal ions, which can be applied towards metal biosensor development. In this study, we investigated the significant fluorescence quenching of Dronpa by Co2+ and Cu2+ ions. Crystal structures of Co2+-, Ni2+- and Cu2+ -bound Dronpa revealed previously unseen, unique, metal-binding sites for fluorescence quenching. These metal ions commonly interact with surface-exposed histidine residues (His194-His210 and His210-His212), and interact indirectly with chromophores. Structural analysis of the Co2+- and Cu2+- binding sites of Dronpa provides insight into FP-based metal biosensor engineering.",

keywords = "biosensor, Dronpa, fluorescent protein, metal-binding site, quenching",

author = "Kim, {In Jung} and Sangsoo Kim and Jeahyun Park and Intae Eom and Sunam Kim and Kim, {Jin Hong} and Ha, {Sung Chul} and Kim, {Yeon Gil} and Hwang, {Kwang Yeon} and Nam, {Ki Hyun}",

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doi = "10.1002/1873-3468.12316",

language = "English",

pages = "2982--2990",

journal = "FEBS Letters",

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TY - JOUR

T1 - Crystal structures of Dronpa complexed with quenchable metal ions provide insight into metal biosensor development

AU - Kim, In Jung

AU - Kim, Sangsoo

AU - Park, Jeahyun

AU - Eom, Intae

AU - Kim, Sunam

AU - Kim, Jin Hong

AU - Ha, Sung Chul

AU - Kim, Yeon Gil

AU - Hwang, Kwang Yeon

AU - Nam, Ki Hyun

PY - 2016/9/1

Y1 - 2016/9/1

N2 - Many fluorescent proteins (FPs) show fluorescence quenching by specific metal ions, which can be applied towards metal biosensor development. In this study, we investigated the significant fluorescence quenching of Dronpa by Co2+ and Cu2+ ions. Crystal structures of Co2+-, Ni2+- and Cu2+ -bound Dronpa revealed previously unseen, unique, metal-binding sites for fluorescence quenching. These metal ions commonly interact with surface-exposed histidine residues (His194-His210 and His210-His212), and interact indirectly with chromophores. Structural analysis of the Co2+- and Cu2+- binding sites of Dronpa provides insight into FP-based metal biosensor engineering.

AB - Many fluorescent proteins (FPs) show fluorescence quenching by specific metal ions, which can be applied towards metal biosensor development. In this study, we investigated the significant fluorescence quenching of Dronpa by Co2+ and Cu2+ ions. Crystal structures of Co2+-, Ni2+- and Cu2+ -bound Dronpa revealed previously unseen, unique, metal-binding sites for fluorescence quenching. These metal ions commonly interact with surface-exposed histidine residues (His194-His210 and His210-His212), and interact indirectly with chromophores. Structural analysis of the Co2+- and Cu2+- binding sites of Dronpa provides insight into FP-based metal biosensor engineering.

KW - biosensor

KW - Dronpa

KW - fluorescent protein

KW - metal-binding site

KW - quenching

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U2 - 10.1002/1873-3468.12316

DO - 10.1002/1873-3468.12316

M3 - Letter

C2 - 27433793

SN - 0014-5793

SP - 2982

EP - 2990

JO - FEBS Letters

JF - FEBS Letters

ER -

Crystal structures of Dronpa complexed with quenchable metal ions provide insight into metal biosensor development

Abstract

Keywords

ASJC Scopus subject areas

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