Thermodynamic and structural characterization of the specific binding of Zn(II) to human protein DJ-1

Shinya Tashiro; Jose M.M. Caaveiro; Chun Xiang Wu; Quyen Q. Hoang; Kouhei Tsumoto

doi:10.1021/bi500294h

Thermodynamic and structural characterization of the specific binding of Zn(II) to human protein DJ-1

Shinya Tashiro, Jose M.M. Caaveiro, Chun Xiang Wu, Quyen Q. Hoang, Kouhei Tsumoto

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

13 Citations (Scopus)

Abstract

Mutations of DJ-1 cause familial Parkinson's disease (PD), although the role of DJ-1 in PD remains unresolved. Very recent reports have shown that DJ-1 interacts with copper ions. This evidence opens new avenues to understanding the function of DJ-1 and its role in PD. Herein, we report that Zn(II) binds to DJ-1 with great selectivity among the other metals examined: Mn(II), Fe(II), Co(II), Ni(II), and Cu(II). High-resolution X-ray crystallography (1.18 Å resolution) shows Zn(II) is coordinated to the protein by the key residues Cys106 and Glu18. These results suggest that DJ-1 may be regulated and/or stabilized by Zn(II).

Original language	English
Pages (from-to)	2218-2220
Number of pages	3
Journal	Biochemistry
Volume	53
Issue number	14
DOIs	https://doi.org/10.1021/bi500294h
Publication status	Published - Apr 15 2014
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry

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10.1021/bi500294h

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title = "Thermodynamic and structural characterization of the specific binding of Zn(II) to human protein DJ-1",

abstract = "Mutations of DJ-1 cause familial Parkinson's disease (PD), although the role of DJ-1 in PD remains unresolved. Very recent reports have shown that DJ-1 interacts with copper ions. This evidence opens new avenues to understanding the function of DJ-1 and its role in PD. Herein, we report that Zn(II) binds to DJ-1 with great selectivity among the other metals examined: Mn(II), Fe(II), Co(II), Ni(II), and Cu(II). High-resolution X-ray crystallography (1.18 {\AA} resolution) shows Zn(II) is coordinated to the protein by the key residues Cys106 and Glu18. These results suggest that DJ-1 may be regulated and/or stabilized by Zn(II).",

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doi = "10.1021/bi500294h",

language = "English",

volume = "53",

pages = "2218--2220",

journal = "Biochemistry",

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T1 - Thermodynamic and structural characterization of the specific binding of Zn(II) to human protein DJ-1

AU - Tashiro, Shinya

AU - Caaveiro, Jose M.M.

AU - Wu, Chun Xiang

AU - Hoang, Quyen Q.

AU - Tsumoto, Kouhei

PY - 2014/4/15

Y1 - 2014/4/15

N2 - Mutations of DJ-1 cause familial Parkinson's disease (PD), although the role of DJ-1 in PD remains unresolved. Very recent reports have shown that DJ-1 interacts with copper ions. This evidence opens new avenues to understanding the function of DJ-1 and its role in PD. Herein, we report that Zn(II) binds to DJ-1 with great selectivity among the other metals examined: Mn(II), Fe(II), Co(II), Ni(II), and Cu(II). High-resolution X-ray crystallography (1.18 Å resolution) shows Zn(II) is coordinated to the protein by the key residues Cys106 and Glu18. These results suggest that DJ-1 may be regulated and/or stabilized by Zn(II).

AB - Mutations of DJ-1 cause familial Parkinson's disease (PD), although the role of DJ-1 in PD remains unresolved. Very recent reports have shown that DJ-1 interacts with copper ions. This evidence opens new avenues to understanding the function of DJ-1 and its role in PD. Herein, we report that Zn(II) binds to DJ-1 with great selectivity among the other metals examined: Mn(II), Fe(II), Co(II), Ni(II), and Cu(II). High-resolution X-ray crystallography (1.18 Å resolution) shows Zn(II) is coordinated to the protein by the key residues Cys106 and Glu18. These results suggest that DJ-1 may be regulated and/or stabilized by Zn(II).

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Thermodynamic and structural characterization of the specific binding of Zn(II) to human protein DJ-1

Abstract

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