Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP

Journal of Molecular Biology

Volumn 355, Issue 5, 2006, Pages 980-988

  Li, Jixi ^a   Wei, Zhiyi ^b   Zheng, Mei ^a   Gu, Xing ^a   Deng, Yingfeng ^a   Qiu, Rui ^a   Chen, Fei ^a   Ji, Chaoneng ^a   Gong, Weimin ^b   Xie, Yi ^a   Mao, Yumin ^a  

^a FUDAN UNIVERSITY   (China)

^b INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

Crystal structure; GMP; Guanosine monophosphate reductase 2; Purine salvage

Indexed keywords

GUANOSINE MONOPHOSPHATE REDUCTASE 2; GUANOSINE PHOSPHATE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATION; CRYSTAL STRUCTURE; DEAMINATION; ENZYME MECHANISM; ENZYME STRUCTURE; HUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; REDUCTION; SEQUENCE ANALYSIS;

EID: 29444450245     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.11.047     Document Type: Article

References (37)

1. J. Neuhard, and P. Nygaard Purines and Pyrimidines F.C. Neidhardt J.L. Ingraham K.B. Low B. Magasanik M. Schaechter E. Umbarger Escherichia coli and Salmonella typhimurium Cellular and Molecular Biology vol. 1 1987 American Society for Microbiology Washington, DC 445 473
2. R.L. Berens, E.C. Krug, and J.J. Marr J.J. Marr M. Muller Biochemistry and Molecular Biology of Parasites 1995 Academic Press London 89 117
3. J.T. Beck, S. Zhao, and C.C. Wang Cloning, sequencing and structural analysis of the DNA encoding inosine monophosphate dehydrogenase (EC 1.1.1.205) from Tritrichomonas foetus Expt. Parasitol. 78 1994 101 112
4. S.C. Andrews, and J.R. Guest Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12 Biochem. J. 255 1988 35 43
5. R.W. Stephens, and V.K. Whittaker Calf thymus GMP reductase: control by XMP Biochem. Biophys. Res. Commun. 53 1973 975 981
6. J.J. Mackenzie, and L.B. Sorensen Guanosine 5′-phosphate reductase of human erythrocytes Biochem. Biophys. Acta 327 1973 282 294
7. T. Spector, T.E. Jones, and R.L. Miller Reaction mechanism, and specificity of human GMP reductase: substrates, inhibitors, activators and inactivators J. Biol. Chem. 254 1979 2308 2315
8. Y. Deng, Z. Wang, K. Ying, S. Gu, C. Ji, and Y. Huang NADPH-dependent GMP reductase isoenzyme of human (GMPR2): expression, purification, and kinetic properties Int. J. Biochem. Cell Biol. 34 2002 1035 1050
9. D. Salvatore, T. Bartha, and P.R. Larsen The guanosine monophosphate reductase gene is conserved in rats and its expression increases rapidly in brown adipose tissue during cold exposure J. Biol. Chem. 273 1998 31092 31096
10. J. Zhang, W. Zhang, D. Zou, G. Chen, T. Wan, M. Zhang, and X. Cao Cloning and functional characterization of GMPR2, a novel human guanosine monophosphate reductase, which promotes the monocytic differentiation of HL-60 leukemia cells J. Cancer Res. Clin. Oncol. 129 2003 76 83
11. A. Becerra, and A. Lazcano The role of gene duplication in the evolution of purine nucleotide salvage pathways Orig. Life Evol. Biosph. 28 1998 539 553
12. G.D. Markham, C.L. Bock, and C. Schalk-Hihi Acid-base catalysis in the chemical mechanism of inosine monophosphate dehydrogenase Biochemistry 38 1999 4433 4440
13. F.M. McMillan, M. Cahoon, A. White, L. Hedstrom, G.A. Petsko, and D. Ringe Crystal structure at 2.4 Å resolution of Borrelia burgdorferi inosine 5′-monophosphate dehydrogenase: evidence of a substrate-induced hinged-lid motion by loop 6 Biochemistry 39 2000 4533 4542
14. M.D. Sintchak, M.A. Fleming, O. Futer, S.A. Raybuck, S.P. Chambers, and P.R. Caron Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid Cell 85 1996 921 930
15. L. Gan, G.A. Petsko, and L. Hedstrom Crystal structure of a ternary complex of Tritrichomonas foetus inosine 5′-monophosphate dehydrogenase: NAD+ orients the active site loop for catalysis Biochemistry 41 2002 13309 13317
16. L. Gan, M.R. Seyedsayamdost, S. Shuto, A. Matsuda, G.A. Petsko, and L. Hedstrom The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase Biochemistry 42 2003 857 863
17. R. Zhang, G. Evans, F.J. Rotella, E.M. Westbrook, D. Beno, and E. Huberman Characteristics and crystal structure of bacterial inosine-5′- monophosphate dehydrogenase Biochemistry 38 1999 4691 4700
18. F.G. Whitby, H. Luecke, P. Kuhn, J.R. Somoza, J.A. Huete-Perez, and J.D. Phillips Crystal structure of Tritrichomonas foetus inosine-5′- monophosphate dehydrogenase and the enzyme-product complex Biochemistry 36 1997 10666 10674
19. T.D. Colby, K. Vanderveen, M.D. Strickler, G.D. Markham, and B.M. Goldstein Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design Proc. Natl Acad. Sci. USA 96 1999 3531 3536
20. A. Hiniker, and J.C. Bardwell Disulfide bond isomerization in prokaryotes Biochemistry 42 2003 1179 1185
21. M. Molinari, and A. Helenius Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells Nature 402 1999 90 93
22. N. Nagano, C.A. Orengo, and J.M. Thornton One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions J. Mol. Biol. 321 2002 741 765
23. G.L. Prosise, and H. Luecke Crystal structures of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with substrate, cofactor and analogs: a structural basis for the random-in ordered-out kinetic mechanism J. Mol. Biol. 326 2003 517 527
24. L. Gan, M.R. Seyedsayamdost, S. Shuto, A. Matsuda, G.A. Petsko, and L. Hedstrom The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase Biochemistry 42 2003 857 863
25. J.A. Huete-Perez, J.C. Wu, F.G. Whitby, and C.C. Wang Identification of the IMP binding site in the IMP dehydrogenase from Tritrichomonas foetus Biochemistry 34 1995 13889 13894
26. L.C. Antonino, K. Straub, and J.C. Wu Probing the active site of human IMP dehydrogenase using halogenated purine riboside 5′-monophosphates and covalent modification reagents Biochemistry 33 1994 1760 1765
27. C.N. Ji, G. Ying, Y.F. Deng, S. Chen, W.H. Zhang, and G. Shu Purification, crystallization and preliminary X-ray studies of GMP reductase 2 from human Acta Crystallog. sect. D 59 2003 1109 1110
28. E. Potterton, P. Briggs, M. Turkenburg, and E. Dodson A graphical user interface to the CCP4 program suite Acta Crystallog. sect. D 59 2003 1131 1137
29. A.T. Brunger, P.D. Adams, G.M. Clore, W.L. DeLano, P. Gros, and R.W. Grosse-Kunstleve Crystallography & NMR system: a new software suite for macromolecular structure determination Acta Crystallog. sect. D 54 1998 905 921
30. A.G.W. Leslie MOSFLM User Guide 1994 MRC-LMB Cambridge
31. R. Laskowski, M. Macarthur, D. Moss, and J. Thornton Procheck - a program to check stereochemical quality of protein structures J. Appl. Crystallog. 26 1993 283 290
32. S.F. Altschul, T.L. Madden, A.A. Schaffer, J. Zhang, Z. Zhang, W. Miller, and D.J. Lipman Gapped BLAST and PSI-BLAST: a new generation of protein database search programs Nucl. Acids Res. 25 1997 3389 3402
33. J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W.: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucl. Acids Res. 22 1994 4673 4680
34. E. Krissinel, and K. Henrick Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallog. sect. D 60 2004 2256 2268
35. M. Carson Ribbons Methods Enzymol. 277 1997 493 505
36. P. Gouet, E. Courcelle, D.I. Stuart, and F. Metoz ESPript: analysis of multiple sequence alignments in PostScript Bioinformatics 15 1999 305 308
37. W. Kabsch, and C. Sander Biopolymers 22 1983 2577 2637