메뉴 건너뛰기




Volumn 46, Issue 17, 2007, Pages 5050-5062

A novel function for the N-terminal nucleophile hydrolase fold demonstrated by the structure of an archaeal inosine monophosphate cyclohydrolase

Author keywords

[No Author keywords available]

Indexed keywords

5-AMINOIMIDAZOLE-4-CARBOXAMIDE RIBONUCLEOTIDE (AICAR); ACTIVE SITES; DE NOVO PURINE BIOSYNTHESIS; GENE PRODUCTS;

EID: 34247645918     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061637j     Document Type: Article
Times cited : (17)

References (48)
  • 1
    • 0030034702 scopus 로고    scopus 로고
    • The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping
    • Rayl, E. A., Moroson, B. A., and Beardsley, G. P. (1996) The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping, J. Biol. Chem. 271, 2225-2233.
    • (1996) J. Biol. Chem , vol.271 , pp. 2225-2233
    • Rayl, E.A.1    Moroson, B.A.2    Beardsley, G.P.3
  • 2
    • 0035032121 scopus 로고    scopus 로고
    • Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis
    • Greasley, S. E., Horton, P., Ramcharan, J., Beardsley, G. P., Benkovic, S. J., and Wilson, I. A. (2001) Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis. Nat. Struct. Biol. 8, 402-406.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 402-406
    • Greasley, S.E.1    Horton, P.2    Ramcharan, J.3    Beardsley, G.P.4    Benkovic, S.J.5    Wilson, I.A.6
  • 3
    • 0842327142 scopus 로고    scopus 로고
    • Structural insights into the human and avian IMP cyclohydrolase mechanism via crystal structures with the bound XMP inhibitor
    • Wolan, D. W., Cheong, C. G., Greasley, S. E., and Wilson, I. A. (2004) Structural insights into the human and avian IMP cyclohydrolase mechanism via crystal structures with the bound XMP inhibitor, Biochemistry 43, 1171-1183.
    • (2004) Biochemistry , vol.43 , pp. 1171-1183
    • Wolan, D.W.1    Cheong, C.G.2    Greasley, S.E.3    Wilson, I.A.4
  • 4
    • 0030925484 scopus 로고    scopus 로고
    • Purine biosynthesis in the domain Archaea without folates or modified folates
    • White, R. H. (1997) Purine biosynthesis in the domain Archaea without folates or modified folates, J. Bacteriol. 179, 3374-3377.
    • (1997) J. Bacteriol , vol.179 , pp. 3374-3377
    • White, R.H.1
  • 6
    • 0036177599 scopus 로고    scopus 로고
    • New class of IMP cyclohydrolases in Methanococcus jannaschii
    • Graupner, M., Xu, H., and White, R. H. (2002) New class of IMP cyclohydrolases in Methanococcus jannaschii, J. Bacteriol. 184, 1471-1473.
    • (2002) J. Bacteriol , vol.184 , pp. 1471-1473
    • Graupner, M.1    Xu, H.2    White, R.H.3
  • 7
    • 15744402488 scopus 로고    scopus 로고
    • A Methanocaldococcus jannaschii archaeal signature gene encodes for a 5-formaminoimidazole-4- carboxamide-1-β-D-ribofuranosyl 5′-monophosphate synthetase. A new enzyme in purine biosynthesis
    • Ownby, K., Xu, H., and White, R. H. (2005) A Methanocaldococcus jannaschii archaeal signature gene encodes for a 5-formaminoimidazole-4- carboxamide-1-β-D-ribofuranosyl 5′-monophosphate synthetase. A new enzyme in purine biosynthesis, J. Biol. Chem. 280, 10881-10887.
    • (2005) J. Biol. Chem , vol.280 , pp. 10881-10887
    • Ownby, K.1    Xu, H.2    White, R.H.3
  • 9
    • 0036643434 scopus 로고    scopus 로고
    • Crystal structure of Methanobacterium thermoautotrophicum conserved protein MTH1020 reveals an NTN-hydrolase fold
    • Saridakis, V., Christendat, D., Thygesen, A., Arrowsmith, C. H., Edwards, A. M., and Pai, E. F. (2002) Crystal structure of Methanobacterium thermoautotrophicum conserved protein MTH1020 reveals an NTN-hydrolase fold, Proteins 48, 141-143.
    • (2002) Proteins , vol.48 , pp. 141-143
    • Saridakis, V.1    Christendat, D.2    Thygesen, A.3    Arrowsmith, C.H.4    Edwards, A.M.5    Pai, E.F.6
  • 10
    • 0034495297 scopus 로고    scopus 로고
    • Structural comparison of NTN-hydrolases
    • Oinonen, C., and Rouvinen, J. (2000) Structural comparison of NTN-hydrolases, Protein Sci. 9, 2329-2337.
    • (2000) Protein Sci , vol.9 , pp. 2329-2337
    • Oinonen, C.1    Rouvinen, J.2
  • 11
    • 22544460277 scopus 로고    scopus 로고
    • Base catalysis of chromophore formation in Arg96 and Glu222 variants of green fluorescent protein
    • Sniegowski, J. A., Lappe, J. W., Patel, H. N., Huffman, H. A., and Wachter, R. M. (2005) Base catalysis of chromophore formation in Arg96 and Glu222 variants of green fluorescent protein, J. Biol. Chem. 280, 26248-26255.
    • (2005) J. Biol. Chem , vol.280 , pp. 26248-26255
    • Sniegowski, J.A.1    Lappe, J.W.2    Patel, H.N.3    Huffman, H.A.4    Wachter, R.M.5
  • 12
    • 0001113167 scopus 로고    scopus 로고
    • Flaks, J. G., Erwin, M. J., and Buchanan, J. M. (1957) Biosynthesis of the purines. XVIII. 5-Amino-1-ribosyl-4-imidazolecarboxamide 5′-phosphate transformylase and inosinicase, J. Biol. Chem. 229, 603-612.
    • Flaks, J. G., Erwin, M. J., and Buchanan, J. M. (1957) Biosynthesis of the purines. XVIII. 5-Amino-1-ribosyl-4-imidazolecarboxamide 5′-phosphate transformylase and inosinicase, J. Biol. Chem. 229, 603-612.
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 15
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B. W. (1968) Solvent content of protein crystals, J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 17
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for the building of protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 18
    • 0002700643 scopus 로고
    • Halloween mask and bones
    • Bailey, S, Hubbard, R, and Waller, D, Eds, pp, SERC Daresbury Laboratory, Warrington, U.K
    • Kleywegt, G. J., and Jones, T. A. (1994) Halloween mask and bones, in From First Map to Final Model (Bailey, S., Hubbard, R., and Waller, D., Eds.) pp 59-66, SERC Daresbury Laboratory, Warrington, U.K.
    • (1994) From First Map to Final Model , pp. 59-66
    • Kleywegt, G.J.1    Jones, T.A.2
  • 19
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 20
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of Molscript which includes greatly enhanced colouring capabilities
    • Esnouf, R. (1997) An extensively modified version of Molscript which includes greatly enhanced colouring capabilities, J. Mol. Graphics 15, 132-134.
    • (1997) J. Mol. Graphics , vol.15 , pp. 132-134
    • Esnouf, R.1
  • 21
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic Molecular Graphics
    • Merritt, E. A., and Bacon, D. J. (1997) Raster3D: Photorealistic Molecular Graphics, Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 23
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. (1997) The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools, Nucleic Acids Res. 24, 4876-4882.
    • (1997) Nucleic Acids Res , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 24
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet, P., Courcelle, E., Stuart, D. I., and Metoz, F. (1999) ESPript: analysis of multiple sequence alignments in PostScript, Bioinformatics 15, 305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 27
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt, G., Woell, S., and Argos, P. (1997) Protein thermal stability, hydrogen bonds, and ion pairs, J. Mol. Biol. 269, 631-643.
    • (1997) J. Mol. Biol , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 28
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • Szilágyi, A., and Závodszky, P. (2000) Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey, Struct. Folding Des. 8, 493-504.
    • (2000) Struct. Folding Des , vol.8 , pp. 493-504
    • Szilágyi, A.1    Závodszky, P.2
  • 29
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2
    • Perutz, M. F., and Raidt, H. (1975) Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2, Nature 255, 256-259.
    • (1975) Nature , vol.255 , pp. 256-259
    • Perutz, M.F.1    Raidt, H.2
  • 30
    • 0019036679 scopus 로고
    • Heat stability of a tetrameric enzyme, D-glyceraldehyde-3-phosphate dehydrogenase
    • Walker, J. E., Wonacott, A. J., and Harris, J. I. (1980) Heat stability of a tetrameric enzyme, D-glyceraldehyde-3-phosphate dehydrogenase, Eur. J. Biochem. 108, 581-586.
    • (1980) Eur. J. Biochem , vol.108 , pp. 581-586
    • Walker, J.E.1    Wonacott, A.J.2    Harris, J.I.3
  • 31
    • 13244249836 scopus 로고
    • The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures
    • Yip, K. S., Stillman, T. J., Britton, K. L., Artymiuk, P. J., Baker, P. J., Sedelnikova, S. E., Engel, P. C., Pasquo, A., Chiaraluce, R., and Consalvi, V. (1995) The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures, Structure 3, 1147-1158.
    • (1995) Structure , vol.3 , pp. 1147-1158
    • Yip, K.S.1    Stillman, T.J.2    Britton, K.L.3    Artymiuk, P.J.4    Baker, P.J.5    Sedelnikova, S.E.6    Engel, P.C.7    Pasquo, A.8    Chiaraluce, R.9    Consalvi, V.10
  • 33
    • 0028027607 scopus 로고
    • 5-Aminoimidazole-4-carboxamide ribotide transformylase-IMP cyclohydrolase from human CCRF-CEM leukemia cells: Purification, pH dependence, and inhibitors
    • Szabados, E., Hindmarsh, E. J., Phillips, L., Duggleby, R. G., and Christopherson, R. I. (1994) 5-Aminoimidazole-4-carboxamide ribotide transformylase-IMP cyclohydrolase from human CCRF-CEM leukemia cells: purification, pH dependence, and inhibitors, Biochemistry 33, 14237-14245.
    • (1994) Biochemistry , vol.33 , pp. 14237-14245
    • Szabados, E.1    Hindmarsh, E.J.2    Phillips, L.3    Duggleby, R.G.4    Christopherson, R.I.5
  • 34
    • 45449097286 scopus 로고
    • Diels-Alder reactions of azadienes
    • Boger, D. L. (1983) Diels-Alder reactions of azadienes, Tetrahedron 39, 2869-2939.
    • (1983) Tetrahedron , vol.39 , pp. 2869-2939
    • Boger, D.L.1
  • 35
    • 0842348744 scopus 로고    scopus 로고
    • Catalytic mechanism of the cyclohydrolase activity of human aminoimidazole carboxamide ribonucleotide formyltransferase/inosine monophosphate cyclohydrolase
    • Vergis, J. M., and Beardsley, G. P. (2004) Catalytic mechanism of the cyclohydrolase activity of human aminoimidazole carboxamide ribonucleotide formyltransferase/inosine monophosphate cyclohydrolase, Biochemistry 43, 1184-1192.
    • (2004) Biochemistry , vol.43 , pp. 1184-1192
    • Vergis, J.M.1    Beardsley, G.P.2
  • 36
    • 0035896591 scopus 로고    scopus 로고
    • Human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine 5′-monophosphate cyclohydrolase. A bifunctional protein requiring dimerization for transformylase activity but not for cyclohydrolase activity
    • Vergis, J. M., Bulock, K. G., Fleming, K. G., and Beardsley, G. P. (2001) Human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine 5′-monophosphate cyclohydrolase. A bifunctional protein requiring dimerization for transformylase activity but not for cyclohydrolase activity, J. Biol. Chem. 276, 7727-7733.
    • (2001) J. Biol. Chem , vol.276 , pp. 7727-7733
    • Vergis, J.M.1    Bulock, K.G.2    Fleming, K.G.3    Beardsley, G.P.4
  • 37
    • 0019884714 scopus 로고
    • On the purification and mechanism of action of 5-aminoimidazole-4-carboxamide-ribonucleotide transformylase from chicken liver
    • Mueller, W. T., and Benkovic, S. J. (1981) On the purification and mechanism of action of 5-aminoimidazole-4-carboxamide-ribonucleotide transformylase from chicken liver, Biochemistry 20, 337-344.
    • (1981) Biochemistry , vol.20 , pp. 337-344
    • Mueller, W.T.1    Benkovic, S.J.2
  • 39
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormo, M., Cubitt, A. B., Kallio, K., Gross, L. A., Tsien, R. Y., and Remington, S. J. (1996) Crystal structure of the Aequorea victoria green fluorescent protein, Science 273, 1392-1395.
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormo, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5    Remington, S.J.6
  • 40
    • 0142027791 scopus 로고    scopus 로고
    • Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures
    • Barondeau, D. P., Putnam, C. D., Kassmann, C. J., Tainer, J. A., and Getzoff, E. D. (2003) Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures, Proc. Natl. Acad. Sci. U.S.A. 100, 12111-12116.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 12111-12116
    • Barondeau, D.P.1    Putnam, C.D.2    Kassmann, C.J.3    Tainer, J.A.4    Getzoff, E.D.5
  • 41
    • 0029920154 scopus 로고    scopus 로고
    • Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site
    • Kim, J. H., Krahn, J. M., Tomchick, D. R., Smith, J. L., and Zalkin, H. (1996) Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site, J. Biol. Chem. 271, 15549-15557.
    • (1996) J. Biol. Chem , vol.271 , pp. 15549-15557
    • Kim, J.H.1    Krahn, J.M.2    Tomchick, D.R.3    Smith, J.L.4    Zalkin, H.5
  • 42
    • 0041624350 scopus 로고    scopus 로고
    • Catalysing new reactions during evolution: Economy of residues and mechanism
    • Bartlett, G. J., Borkakoti, N., and Thornton, J. M. (2003) Catalysing new reactions during evolution: economy of residues and mechanism, J. Mol. Biol. 331, 829-860.
    • (2003) J. Mol. Biol , vol.331 , pp. 829-860
    • Bartlett, G.J.1    Borkakoti, N.2    Thornton, J.M.3
  • 43
    • 0029446407 scopus 로고
    • A sting in the (N-terminal) tail
    • Artymiuk, P. J. (1995) A sting in the (N-terminal) tail, Nat. Struct. Biol. 2, 1035-1037.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 1035-1037
    • Artymiuk, P.J.1
  • 44
  • 45
    • 0037304408 scopus 로고    scopus 로고
    • Emergence of diverse biochemical activities in evolutionarily conserved structural scaffolds of proteins
    • Anantharaman, V., Aravind, L., and Koonin, E. V. (2003) Emergence of diverse biochemical activities in evolutionarily conserved structural scaffolds of proteins, Curr. Opin. Chem. Biol. 7, 12-20.
    • (2003) Curr. Opin. Chem. Biol , vol.7 , pp. 12-20
    • Anantharaman, V.1    Aravind, L.2    Koonin, E.V.3
  • 46
    • 0036384350 scopus 로고    scopus 로고
    • One fold with many functions: The evolutionary relationships between TIM barrel families based on their sequences, structures and functions
    • Nagano, N., Orengo, C. A., and Thornton, J. M. (2002) One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions, J. Mol. Biol. 321, 741-765.
    • (2002) J. Mol. Biol , vol.321 , pp. 741-765
    • Nagano, N.1    Orengo, C.A.2    Thornton, J.M.3
  • 48
    • 0034664991 scopus 로고    scopus 로고
    • Tetrahydrofolate and tetrahydromethanopterin compared: Functionally distinct carriers in C1 metabolism
    • Maden, B. E. (2000) Tetrahydrofolate and tetrahydromethanopterin compared: functionally distinct carriers in C1 metabolism, Biochem. J. 350 (Part 3), 609-629.
    • (2000) Biochem. J , vol.350 , Issue.PART 3 , pp. 609-629
    • Maden, B.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.