Structural analysis of 1-Cys type selenoprotein methionine sulfoxide reductase A

Eun Hye Lee; Geun Hee Kwak; Moon Jung Kim; Hwa Young Kim; Kwang Yeon Hwang

doi:10.1016/j.abb.2013.12.024

Structural analysis of 1-Cys type selenoprotein methionine sulfoxide reductase A

Eun Hye Lee, Geun Hee Kwak, Moon Jung Kim, Hwa Young Kim, Kwang Yeon Hwang

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

12 Citations (Scopus)

Abstract

Methionine sulfoxide reductase A (MsrA) reduces free and protein-based methionine-S-sulfoxide to methionine. Structures of 1-Cys MsrAs lacking a resolving Cys, which interacts with catalytic Cys, are unknown. In addition, no structural information on selenocysteine (Sec)-containing MsrA enzymes has been reported. In this work, we determined the crystal structures of 1-Cys type selenoprotein MsrA from Clostridium oremlandii at 1.6-1.8 Å, including the reduced, oxidized (sulfenic acid), and substrate-bound forms. The overall structure of Clostridium MsrA, consisting of ten α-helices and six β-strands, folds into a catalytic domain and a novel helical domain absent from other known MsrA structures. The helical domain, containing five helices, tightly interacts with the catalytic domain, and is likely critical for catalytic activity due to its association with organizing the active site. This helical domain is also conserved in several selenoprotein MsrAs. Our structural analysis reveals that the side chain length of Glu55 is critical for the proton donor function of this residue. Our structures also provide insights into the architecture of the 1-Cys MsrA active site and the roles of active site residues in substrate recognition and catalysis.

Original language	English
Pages (from-to)	1-8
Number of pages	8
Journal	Archives of Biochemistry and Biophysics
Volume	545
DOIs	https://doi.org/10.1016/j.abb.2013.12.024
Publication status	Published - 2014 Mar 1

Bibliographical note

Funding Information:
We thank the staff of beamlines 4A at the Pohang Accelerator Laboratory and BL1A at the Photon Factory for technical support. We are also grateful to the staff at the Korea Basic Science Institute (Daejeon, Korea) for the use of a mosquito crystallization robot and the Rigaku MicroMax-007HF X-ray generator. This work was supported by grants from the National Research Foundation of Korea (2011-0028166 and 2013-044795).

Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.

Keywords

Catalysis
Clostridium
Methionine sulfoxide reductase
MsrA
Selenocysteine
Selenoprotein

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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10.1016/j.abb.2013.12.024

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@article{9bf912ac41a7466498a6c4b3a99546a5,

title = "Structural analysis of 1-Cys type selenoprotein methionine sulfoxide reductase A",

abstract = "Methionine sulfoxide reductase A (MsrA) reduces free and protein-based methionine-S-sulfoxide to methionine. Structures of 1-Cys MsrAs lacking a resolving Cys, which interacts with catalytic Cys, are unknown. In addition, no structural information on selenocysteine (Sec)-containing MsrA enzymes has been reported. In this work, we determined the crystal structures of 1-Cys type selenoprotein MsrA from Clostridium oremlandii at 1.6-1.8 {\AA}, including the reduced, oxidized (sulfenic acid), and substrate-bound forms. The overall structure of Clostridium MsrA, consisting of ten α-helices and six β-strands, folds into a catalytic domain and a novel helical domain absent from other known MsrA structures. The helical domain, containing five helices, tightly interacts with the catalytic domain, and is likely critical for catalytic activity due to its association with organizing the active site. This helical domain is also conserved in several selenoprotein MsrAs. Our structural analysis reveals that the side chain length of Glu55 is critical for the proton donor function of this residue. Our structures also provide insights into the architecture of the 1-Cys MsrA active site and the roles of active site residues in substrate recognition and catalysis.",

keywords = "Catalysis, Clostridium, Methionine sulfoxide reductase, MsrA, Selenocysteine, Selenoprotein",

author = "Lee, {Eun Hye} and Kwak, {Geun Hee} and Kim, {Moon Jung} and Kim, {Hwa Young} and Hwang, {Kwang Yeon}",

note = "Funding Information: We thank the staff of beamlines 4A at the Pohang Accelerator Laboratory and BL1A at the Photon Factory for technical support. We are also grateful to the staff at the Korea Basic Science Institute (Daejeon, Korea) for the use of a mosquito crystallization robot and the Rigaku MicroMax-007HF X-ray generator. This work was supported by grants from the National Research Foundation of Korea (2011-0028166 and 2013-044795). Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "2014",

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doi = "10.1016/j.abb.2013.12.024",

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AU - Lee, Eun Hye

AU - Kwak, Geun Hee

AU - Kim, Moon Jung

AU - Kim, Hwa Young

AU - Hwang, Kwang Yeon

N1 - Funding Information: We thank the staff of beamlines 4A at the Pohang Accelerator Laboratory and BL1A at the Photon Factory for technical support. We are also grateful to the staff at the Korea Basic Science Institute (Daejeon, Korea) for the use of a mosquito crystallization robot and the Rigaku MicroMax-007HF X-ray generator. This work was supported by grants from the National Research Foundation of Korea (2011-0028166 and 2013-044795). Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 2014/3/1

Y1 - 2014/3/1

N2 - Methionine sulfoxide reductase A (MsrA) reduces free and protein-based methionine-S-sulfoxide to methionine. Structures of 1-Cys MsrAs lacking a resolving Cys, which interacts with catalytic Cys, are unknown. In addition, no structural information on selenocysteine (Sec)-containing MsrA enzymes has been reported. In this work, we determined the crystal structures of 1-Cys type selenoprotein MsrA from Clostridium oremlandii at 1.6-1.8 Å, including the reduced, oxidized (sulfenic acid), and substrate-bound forms. The overall structure of Clostridium MsrA, consisting of ten α-helices and six β-strands, folds into a catalytic domain and a novel helical domain absent from other known MsrA structures. The helical domain, containing five helices, tightly interacts with the catalytic domain, and is likely critical for catalytic activity due to its association with organizing the active site. This helical domain is also conserved in several selenoprotein MsrAs. Our structural analysis reveals that the side chain length of Glu55 is critical for the proton donor function of this residue. Our structures also provide insights into the architecture of the 1-Cys MsrA active site and the roles of active site residues in substrate recognition and catalysis.

AB - Methionine sulfoxide reductase A (MsrA) reduces free and protein-based methionine-S-sulfoxide to methionine. Structures of 1-Cys MsrAs lacking a resolving Cys, which interacts with catalytic Cys, are unknown. In addition, no structural information on selenocysteine (Sec)-containing MsrA enzymes has been reported. In this work, we determined the crystal structures of 1-Cys type selenoprotein MsrA from Clostridium oremlandii at 1.6-1.8 Å, including the reduced, oxidized (sulfenic acid), and substrate-bound forms. The overall structure of Clostridium MsrA, consisting of ten α-helices and six β-strands, folds into a catalytic domain and a novel helical domain absent from other known MsrA structures. The helical domain, containing five helices, tightly interacts with the catalytic domain, and is likely critical for catalytic activity due to its association with organizing the active site. This helical domain is also conserved in several selenoprotein MsrAs. Our structural analysis reveals that the side chain length of Glu55 is critical for the proton donor function of this residue. Our structures also provide insights into the architecture of the 1-Cys MsrA active site and the roles of active site residues in substrate recognition and catalysis.

KW - Catalysis

KW - Clostridium

KW - Methionine sulfoxide reductase

KW - MsrA

KW - Selenocysteine

KW - Selenoprotein

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U2 - 10.1016/j.abb.2013.12.024

DO - 10.1016/j.abb.2013.12.024

M3 - Article

C2 - 24412203

AN - SCOPUS:84893321353

SN - 0003-9861

VL - 545

SP - 1

EP - 8

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

ER -

Structural analysis of 1-Cys type selenoprotein methionine sulfoxide reductase A

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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