Crystallization and preliminary X-ray analysis of human MTH1 complexed with two oxidized nucleotides, 8-oxo-dGMP and 2-oxo-dATP

Teruya Nakamura; Yuki Kitaguchi; Masayuki Miyazawa; Hiroyuki Kamiya; Sachiko Toma; Shinji Ikemizu; Masahiro Shirakawa; Yusaku Nakabeppu; Yuriko Yamagata

doi:10.1107/S1744309106049529

Crystallization and preliminary X-ray analysis of human MTH1 complexed with two oxidized nucleotides, 8-oxo-dGMP and 2-oxo-dATP

Teruya Nakamura, Yuki Kitaguchi, Masayuki Miyazawa, Hiroyuki Kamiya, Sachiko Toma, Shinji Ikemizu, Masahiro Shirakawa, Yusaku Nakabeppu, Yuriko Yamagata

Department of Immunobiology and Neuroscience

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

5 Citations (Scopus)

Abstract

Human MutT homologue 1 (hMTH1) hydrolyzes a variety of oxidized purine nucleoside triphosphates, including 8-oxo-dGTP, 2-oxo-dATP, 2-oxo-ATP and 8-oxo-dATP, to their corresponding nucleoside monophosphates, while Esherichia coli MutT possesses prominent substrate specificity for 8-oxoguanine nucleotides. Three types of crystals were obtained corresponding to the following complexes: selenomethionine-labelled hMTH1 with 8-oxo-dGMP (SeMet hMTH1-8-oxo-dGMP), hMTH1 with 8-oxo-dGMP (hMTH1-8-oxo-dGMP) and hMTH1 with 2-oxo-dATP (hMTH1-2-oxo-dATP). Crystals of the SeMet hMTH1-8-oxo-dGMP complex belong to space group P4₁2₁2, with unit-cell parameters a = b = 45.8, c = 153.6 Å, and diffracted to 2.90 Å. Crystals of hMTH1-8-oxo-dGMP and hMTH1-2-oxo-dATP belong to space groups P2₁ and P2₁2₁2₁, with unit-cell parameters a = 34.0, b = 59.0, c = 65.9 Å, β = 90.7° and a = 59.2, b = 67.3, c = 80.0 Å, respectively. Their diffraction data were collected at resolutions of 1.95 and 2.22 Å, respectively.

Original language	English
Pages (from-to)	1283-1285
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	62
Issue number	12
DOIs	https://doi.org/10.1107/S1744309106049529
Publication status	Published - Dec 2006

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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Nakamura, T., Kitaguchi, Y., Miyazawa, M., Kamiya, H., Toma, S., Ikemizu, S., Shirakawa, M., Nakabeppu, Y., & Yamagata, Y. (2006). Crystallization and preliminary X-ray analysis of human MTH1 complexed with two oxidized nucleotides, 8-oxo-dGMP and 2-oxo-dATP. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(12), 1283-1285. https://doi.org/10.1107/S1744309106049529

Crystallization and preliminary X-ray analysis of human MTH1 complexed with two oxidized nucleotides, 8-oxo-dGMP and 2-oxo-dATP. / Nakamura, Teruya; Kitaguchi, Yuki; Miyazawa, Masayuki; Kamiya, Hiroyuki; Toma, Sachiko; Ikemizu, Shinji; Shirakawa, Masahiro; Nakabeppu, Yusaku; Yamagata, Yuriko.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 62, No. 12, 12.2006, p. 1283-1285.

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

Nakamura, T, Kitaguchi, Y, Miyazawa, M, Kamiya, H, Toma, S, Ikemizu, S, Shirakawa, M, Nakabeppu, Y & Yamagata, Y 2006, 'Crystallization and preliminary X-ray analysis of human MTH1 complexed with two oxidized nucleotides, 8-oxo-dGMP and 2-oxo-dATP', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 62, no. 12, pp. 1283-1285. https://doi.org/10.1107/S1744309106049529

Nakamura, Teruya ; Kitaguchi, Yuki ; Miyazawa, Masayuki ; Kamiya, Hiroyuki ; Toma, Sachiko ; Ikemizu, Shinji ; Shirakawa, Masahiro ; Nakabeppu, Yusaku ; Yamagata, Yuriko. / Crystallization and preliminary X-ray analysis of human MTH1 complexed with two oxidized nucleotides, 8-oxo-dGMP and 2-oxo-dATP. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2006 ; Vol. 62, No. 12. pp. 1283-1285.

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title = "Crystallization and preliminary X-ray analysis of human MTH1 complexed with two oxidized nucleotides, 8-oxo-dGMP and 2-oxo-dATP",

abstract = "Human MutT homologue 1 (hMTH1) hydrolyzes a variety of oxidized purine nucleoside triphosphates, including 8-oxo-dGTP, 2-oxo-dATP, 2-oxo-ATP and 8-oxo-dATP, to their corresponding nucleoside monophosphates, while Esherichia coli MutT possesses prominent substrate specificity for 8-oxoguanine nucleotides. Three types of crystals were obtained corresponding to the following complexes: selenomethionine-labelled hMTH1 with 8-oxo-dGMP (SeMet hMTH1-8-oxo-dGMP), hMTH1 with 8-oxo-dGMP (hMTH1-8-oxo-dGMP) and hMTH1 with 2-oxo-dATP (hMTH1-2-oxo-dATP). Crystals of the SeMet hMTH1-8-oxo-dGMP complex belong to space group P41212, with unit-cell parameters a = b = 45.8, c = 153.6 {\AA}, and diffracted to 2.90 {\AA}. Crystals of hMTH1-8-oxo-dGMP and hMTH1-2-oxo-dATP belong to space groups P21 and P212121, with unit-cell parameters a = 34.0, b = 59.0, c = 65.9 {\AA}, β = 90.7° and a = 59.2, b = 67.3, c = 80.0 {\AA}, respectively. Their diffraction data were collected at resolutions of 1.95 and 2.22 {\AA}, respectively.",

author = "Teruya Nakamura and Yuki Kitaguchi and Masayuki Miyazawa and Hiroyuki Kamiya and Sachiko Toma and Shinji Ikemizu and Masahiro Shirakawa and Yusaku Nakabeppu and Yuriko Yamagata",

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AU - Kitaguchi, Yuki

AU - Miyazawa, Masayuki

AU - Kamiya, Hiroyuki

AU - Toma, Sachiko

AU - Ikemizu, Shinji

AU - Shirakawa, Masahiro

AU - Nakabeppu, Yusaku

AU - Yamagata, Yuriko

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N2 - Human MutT homologue 1 (hMTH1) hydrolyzes a variety of oxidized purine nucleoside triphosphates, including 8-oxo-dGTP, 2-oxo-dATP, 2-oxo-ATP and 8-oxo-dATP, to their corresponding nucleoside monophosphates, while Esherichia coli MutT possesses prominent substrate specificity for 8-oxoguanine nucleotides. Three types of crystals were obtained corresponding to the following complexes: selenomethionine-labelled hMTH1 with 8-oxo-dGMP (SeMet hMTH1-8-oxo-dGMP), hMTH1 with 8-oxo-dGMP (hMTH1-8-oxo-dGMP) and hMTH1 with 2-oxo-dATP (hMTH1-2-oxo-dATP). Crystals of the SeMet hMTH1-8-oxo-dGMP complex belong to space group P41212, with unit-cell parameters a = b = 45.8, c = 153.6 Å, and diffracted to 2.90 Å. Crystals of hMTH1-8-oxo-dGMP and hMTH1-2-oxo-dATP belong to space groups P21 and P212121, with unit-cell parameters a = 34.0, b = 59.0, c = 65.9 Å, β = 90.7° and a = 59.2, b = 67.3, c = 80.0 Å, respectively. Their diffraction data were collected at resolutions of 1.95 and 2.22 Å, respectively.

AB - Human MutT homologue 1 (hMTH1) hydrolyzes a variety of oxidized purine nucleoside triphosphates, including 8-oxo-dGTP, 2-oxo-dATP, 2-oxo-ATP and 8-oxo-dATP, to their corresponding nucleoside monophosphates, while Esherichia coli MutT possesses prominent substrate specificity for 8-oxoguanine nucleotides. Three types of crystals were obtained corresponding to the following complexes: selenomethionine-labelled hMTH1 with 8-oxo-dGMP (SeMet hMTH1-8-oxo-dGMP), hMTH1 with 8-oxo-dGMP (hMTH1-8-oxo-dGMP) and hMTH1 with 2-oxo-dATP (hMTH1-2-oxo-dATP). Crystals of the SeMet hMTH1-8-oxo-dGMP complex belong to space group P41212, with unit-cell parameters a = b = 45.8, c = 153.6 Å, and diffracted to 2.90 Å. Crystals of hMTH1-8-oxo-dGMP and hMTH1-2-oxo-dATP belong to space groups P21 and P212121, with unit-cell parameters a = 34.0, b = 59.0, c = 65.9 Å, β = 90.7° and a = 59.2, b = 67.3, c = 80.0 Å, respectively. Their diffraction data were collected at resolutions of 1.95 and 2.22 Å, respectively.

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ER -

Crystallization and preliminary X-ray analysis of human MTH1 complexed with two oxidized nucleotides, 8-oxo-dGMP and 2-oxo-dATP

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