Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish

Mickael Blaise; Husam Mohammad Ali Baker Alsarraf; Jaslyn Wong; Søren Roi Midtgaard; Fabrice Jean Francois Laroche; Lotte Schack; Herman  Spaink; Jens Stougaard; Søren Skou Thirup

doi:10.1002/prot.24050

Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish

Mickael Blaise, Husam Mohammad Ali Baker Alsarraf, Jaslyn Wong, Søren Roi Midtgaard, Fabrice Jean Francois Laroche, Lotte Schack, Herman Spaink, Jens Stougaard, Søren Skou Thirup

Department of Molecular Biology and Genetics

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

31 Citations (Scopus)

Abstract

The oxidation resistance proteins (OXR) help to protect eukaryotes from reactive oxygen species. The sole C-terminal domain of the OXR, named TLDc is sufficient to perform this function. However, the mechanism by which oxidation resistance occurs is poorly understood. We present here the crystal structure of the TLDc domain of the oxidation resistance protein 2 from zebrafish. The structure was determined by X-ray crystallography to atomic resolution (0.97Å) and adopts an overall globular shape. Two antiparallel β-sheets form a central β-sandwich, surrounded by two helices and two one-turn helices. The fold shares low structural similarity to known structures

Original language	English
Journal	Proteins: Structure, Function, and Bioinformatics
Volume	80
Issue	6
Pages (from-to)	1694-1698
Number of pages	5
ISSN	0887-3585
DOIs	https://doi.org/10.1002/prot.24050
Publication status	Published - Jun 2012

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@article{62097d16ef864691affc190e2ae3a4ec,

title = "Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish",

abstract = "The oxidation resistance proteins (OXR) help to protect eukaryotes from reactive oxygen species. The sole C-terminal domain of the OXR, named TLDc is sufficient to perform this function. However, the mechanism by which oxidation resistance occurs is poorly understood. We present here the crystal structure of the TLDc domain of the oxidation resistance protein 2 from zebrafish. The structure was determined by X-ray crystallography to atomic resolution (0.97{\AA}) and adopts an overall globular shape. Two antiparallel β-sheets form a central β-sandwich, surrounded by two helices and two one-turn helices. The fold shares low structural similarity to known structures",

author = "Mickael Blaise and Alsarraf, {Husam Mohammad Ali Baker} and Jaslyn Wong and {Roi Midtgaard}, S{\o}ren and Laroche, {Fabrice Jean Francois} and Lotte Schack and Herman Spaink and Jens Stougaard and Thirup, {S{\o}ren Skou}",

year = "2012",

month = jun,

doi = "10.1002/prot.24050",

language = "English",

volume = "80",

pages = "1694--1698",

journal = "Proteins: Structure, Function, and Bioinformatics",

issn = "0887-3585",

publisher = "John Wiley & Sons Inc.",

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}

Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish. / Blaise, Mickael; Alsarraf, Husam Mohammad Ali Baker; Wong, Jaslyn et al.
In: Proteins: Structure, Function, and Bioinformatics, Vol. 80, No. 6, 06.2012, p. 1694-1698.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

TY - JOUR

T1 - Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish

AU - Blaise, Mickael

AU - Alsarraf, Husam Mohammad Ali Baker

AU - Wong, Jaslyn

AU - Roi Midtgaard, Søren

AU - Laroche, Fabrice Jean Francois

AU - Schack, Lotte

AU - Spaink, Herman

AU - Stougaard, Jens

AU - Thirup, Søren Skou

PY - 2012/6

Y1 - 2012/6

N2 - The oxidation resistance proteins (OXR) help to protect eukaryotes from reactive oxygen species. The sole C-terminal domain of the OXR, named TLDc is sufficient to perform this function. However, the mechanism by which oxidation resistance occurs is poorly understood. We present here the crystal structure of the TLDc domain of the oxidation resistance protein 2 from zebrafish. The structure was determined by X-ray crystallography to atomic resolution (0.97Å) and adopts an overall globular shape. Two antiparallel β-sheets form a central β-sandwich, surrounded by two helices and two one-turn helices. The fold shares low structural similarity to known structures

AB - The oxidation resistance proteins (OXR) help to protect eukaryotes from reactive oxygen species. The sole C-terminal domain of the OXR, named TLDc is sufficient to perform this function. However, the mechanism by which oxidation resistance occurs is poorly understood. We present here the crystal structure of the TLDc domain of the oxidation resistance protein 2 from zebrafish. The structure was determined by X-ray crystallography to atomic resolution (0.97Å) and adopts an overall globular shape. Two antiparallel β-sheets form a central β-sandwich, surrounded by two helices and two one-turn helices. The fold shares low structural similarity to known structures

U2 - 10.1002/prot.24050

DO - 10.1002/prot.24050

M3 - Journal article

C2 - 22434723

SN - 0887-3585

VL - 80

SP - 1694

EP - 1698

JO - Proteins: Structure, Function, and Bioinformatics

JF - Proteins: Structure, Function, and Bioinformatics

IS - 6

ER -

Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish

Abstract

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