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

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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 languageEnglish
Pages (from-to)1283-1285
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume62
Issue number12
DOIs
Publication statusPublished - Dec 1 2006

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All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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