Crystallization and preliminary X-ray analysis of human MTH1 complexed with two oxidized nucleotides, 8-oxo-dGMP and 2-oxo-dATP.
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 Escherichia 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 P4(1)2(1)2, with unit-cell parameters a = b = 45.8, c = 153.6 A, and diffracted to 2.90 A. Crystals of hMTH1-8-oxo-dGMP and hMTH1-2-oxo-dATP belong to space groups P2(1) and P2(1)2(1)2(1), with unit-cell parameters a = 34.0, b = 59.0, c = 65.9 A, beta = 90.7 degrees and a = 59.2, b = 67.3, c = 80.0 A, respectively. Their diffraction data were collected at resolutions of 1.95 and 2.22 A, respectively.
Nakamura
Teruya
T
Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto 862-0973, Japan.
Kitaguchi
Yuki
Y
Miyazawa
Masayuki
M
Kamiya
Hiroyuki
H
Toma
Sachiko
S
Ikemizu
Shinji
S
Shirakawa
Masahiro
M
Nakabeppu
Yusaku
Y
Yamagata
Yuriko
Y
D003460:Crystallization; D018360:Crystallography, X-Ray; D045643:DNA Repair Enzymes / Q000737:chemistry*; D003838:Deoxyadenine Nucleotides / Q000737:chemistry*; D006157:Guanosine Monophosphate / Q000031:analogs & derivatives* / Q000737:chemistry; D006801:Humans; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry*
C515742:8-oxo-7,8-dihydro-2'-deoxyguanosine-5'-monophosphate; C089930:8-oxodeoxyadenosine triphosphate; D003838:Deoxyadenine Nucleotides; D006157:Guanosine Monophosphate; D010744:Phosphoric Monoester Hydrolases; C078207:8-oxodGTPase; D045643:DNA Repair Enzymes