메뉴 건너뛰기




Volumn 376, Issue 2, 2008, Pages 506-516

A Rationally Designed Monomeric Variant of Anthranilate Phosphoribosyltransferase from Sulfolobus solfataricus is as Active as the Dimeric Wild-type Enzyme but Less Thermostable

Author keywords

anthranilate phosphoribosyltransferase; hyperthermophile; rational protein design; Sulfolobus solfataricus; thermal stability

Indexed keywords

ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; ENZYME VARIANT; MONOMER;

EID: 38349132546     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.11.078     Document Type: Article
Times cited : (23)

References (45)
  • 1
    • 0033617187 scopus 로고    scopus 로고
    • The molecular basis of substrate channeling
    • Miles E.W., Rhee S., and Davies D.R. The molecular basis of substrate channeling. J. Biol. Chem. 274 (1999) 12193-12196
    • (1999) J. Biol. Chem. , vol.274 , pp. 12193-12196
    • Miles, E.W.1    Rhee, S.2    Davies, D.R.3
  • 3
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke R., and Böhm G. The stability of proteins in extreme environments. Curr. Opin. Struct. Biol. 8 (1998) 738-748
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 738-748
    • Jaenicke, R.1    Böhm, G.2
  • 5
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability
    • Vieille C., and Zeikus G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 65 (2001) 1-43
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 7
    • 0030857332 scopus 로고    scopus 로고
    • A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability
    • Schliebs W., Thanki N., Jaenicke R., and Wierenga R.K. A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability. Biochemistry 36 (1997) 9655-9662
    • (1997) Biochemistry , vol.36 , pp. 9655-9662
    • Schliebs, W.1    Thanki, N.2    Jaenicke, R.3    Wierenga, R.K.4
  • 8
    • 0034654087 scopus 로고    scopus 로고
    • Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima
    • Thoma R., Hennig M., Sterner R., and Kirschner K. Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima. Structure Fold. Des. 8 (2000) 265-276
    • (2000) Structure Fold. Des. , vol.8 , pp. 265-276
    • Thoma, R.1    Hennig, M.2    Sterner, R.3    Kirschner, K.4
  • 9
    • 0036839243 scopus 로고    scopus 로고
    • The dimeric dihydroorotate dehydrogenase A from Lactococcus lactis dissociates reversibly into inactive monomers
    • Ottosen M.B., Bjornberg O., Norager S., Larsen S., Palfey B.A., and Jensen K.F. The dimeric dihydroorotate dehydrogenase A from Lactococcus lactis dissociates reversibly into inactive monomers. Protein Sci. 11 (2002) 2575-2583
    • (2002) Protein Sci. , vol.11 , pp. 2575-2583
    • Ottosen, M.B.1    Bjornberg, O.2    Norager, S.3    Larsen, S.4    Palfey, B.A.5    Jensen, K.F.6
  • 10
    • 4944265460 scopus 로고    scopus 로고
    • Effect of dimer dissociation on activity and thermostability of the α-glucuronidase from Geobacillus stearothermophilus: dissecting the different oligomeric forms of family 67 glycoside hydrolases
    • Shallom D., Golan G., Shoham G., and Shoham Y. Effect of dimer dissociation on activity and thermostability of the α-glucuronidase from Geobacillus stearothermophilus: dissecting the different oligomeric forms of family 67 glycoside hydrolases. J. Bacteriol. 186 (2004) 6928-6937
    • (2004) J. Bacteriol. , vol.186 , pp. 6928-6937
    • Shallom, D.1    Golan, G.2    Shoham, G.3    Shoham, Y.4
  • 11
    • 33144457631 scopus 로고    scopus 로고
    • Double mutation at the subunit interface of glutathione transferase rGSTM1-1 results in a stable, folded monomer
    • Thompson L.C., Walters J., Burke J., Parsons J.F., Armstrong R.N., and Dirr H.W. Double mutation at the subunit interface of glutathione transferase rGSTM1-1 results in a stable, folded monomer. Biochemistry 45 (2006) 2267-2273
    • (2006) Biochemistry , vol.45 , pp. 2267-2273
    • Thompson, L.C.1    Walters, J.2    Burke, J.3    Parsons, J.F.4    Armstrong, R.N.5    Dirr, H.W.6
  • 13
    • 0032534756 scopus 로고    scopus 로고
    • Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: a potential TB drug target
    • Sharma V., Grubmeyer C., and Sacchettini J.C. Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: a potential TB drug target. Structure 6 (1998) 1587-1599
    • (1998) Structure , vol.6 , pp. 1587-1599
    • Sharma, V.1    Grubmeyer, C.2    Sacchettini, J.C.3
  • 14
    • 0031568330 scopus 로고    scopus 로고
    • A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase
    • Eads J.C., Ozturk D., Wexler T.B., Grubmeyer C., and Sacchettini J.C. A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase. Structure 5 (1997) 47-58
    • (1997) Structure , vol.5 , pp. 47-58
    • Eads, J.C.1    Ozturk, D.2    Wexler, T.B.3    Grubmeyer, C.4    Sacchettini, J.C.5
  • 15
    • 24044512630 scopus 로고    scopus 로고
    • Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum
    • Shin D.H., Oganesyan N., Jancarik J., Yokota H., Kim R., and Kim S.H. Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum. J. Biol. Chem. 280 (2005) 18326-18335
    • (2005) J. Biol. Chem. , vol.280 , pp. 18326-18335
    • Shin, D.H.1    Oganesyan, N.2    Jancarik, J.3    Yokota, H.4    Kim, R.5    Kim, S.H.6
  • 16
    • 0036645661 scopus 로고    scopus 로고
    • Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry
    • Mayans O., Ivens A., Nissen L.J., Kirschner K., and Wilmanns M. Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry. EMBO J. 21 (2002) 3245-3254
    • (2002) EMBO J. , vol.21 , pp. 3245-3254
    • Mayans, O.1    Ivens, A.2    Nissen, L.J.3    Kirschner, K.4    Wilmanns, M.5
  • 17
    • 0037125240 scopus 로고    scopus 로고
    • The crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum
    • Kim C., Xuong N.H., Edwards S., Yee M.C., Spraggon G., and Mills S.E. The crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum. FEBS Letters 523 (2002) 239-246
    • (2002) FEBS Letters , vol.523 , pp. 239-246
    • Kim, C.1    Xuong, N.H.2    Edwards, S.3    Yee, M.C.4    Spraggon, G.5    Mills, S.E.6
  • 18
    • 29144495844 scopus 로고    scopus 로고
    • The crystal structure of TrpD, a metabolic enzyme essential for lung colonization by Mycobacterium tuberculosis, in complex with its substrate phosphoribosylpyrophosphate
    • Lee C.E., Goodfellow C., Javid-Majd F., Baker E.N., and Shaun Lott J. The crystal structure of TrpD, a metabolic enzyme essential for lung colonization by Mycobacterium tuberculosis, in complex with its substrate phosphoribosylpyrophosphate. J. Mol. Biol. 355 (2006) 784-797
    • (2006) J. Mol. Biol. , vol.355 , pp. 784-797
    • Lee, C.E.1    Goodfellow, C.2    Javid-Majd, F.3    Baker, E.N.4    Shaun Lott, J.5
  • 19
    • 0036183496 scopus 로고    scopus 로고
    • Structural analyses reveal two distinct families of nucleoside phosphorylases
    • Pugmire M.J., and Ealick S.E. Structural analyses reveal two distinct families of nucleoside phosphorylases. Biochem. J. 361 (2002) 1-25
    • (2002) Biochem. J. , vol.361 , pp. 1-25
    • Pugmire, M.J.1    Ealick, S.E.2
  • 20
    • 33746371711 scopus 로고    scopus 로고
    • Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus
    • Marino M., Deuss M., Svergun D.I., Konarev P.V., Sterner R., and Mayans O. Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus. J. Biol. Chem. 281 (2006) 21410-21421
    • (2006) J. Biol. Chem. , vol.281 , pp. 21410-21421
    • Marino, M.1    Deuss, M.2    Svergun, D.I.3    Konarev, P.V.4    Sterner, R.5    Mayans, O.6
  • 21
    • 0035012406 scopus 로고    scopus 로고
    • Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus
    • Ivens A., Mayans O., Szadkowski H., Wilmanns M., and Kirschner K. Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus. Eur. J. Biochem. 268 (2001) 2246-2252
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2246-2252
    • Ivens, A.1    Mayans, O.2    Szadkowski, H.3    Wilmanns, M.4    Kirschner, K.5
  • 22
    • 13444254300 scopus 로고    scopus 로고
    • PDBsum more: new summaries and analyses of the known 3D structures of proteins and nucleic acids
    • Laskowski R.A., Chistyakov V.V., and Thornton J.M. PDBsum more: new summaries and analyses of the known 3D structures of proteins and nucleic acids. Nucl. Acids Res. 33 (2005) D266-D268
    • (2005) Nucl. Acids Res. , vol.33
    • Laskowski, R.A.1    Chistyakov, V.V.2    Thornton, J.M.3
  • 23
    • 33846374339 scopus 로고    scopus 로고
    • Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa
    • Trevino S.R., Scholtz J.M., and Pace C.N. Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa. J. Mol. Biol. 366 (2007) 449-460
    • (2007) J. Mol. Biol. , vol.366 , pp. 449-460
    • Trevino, S.R.1    Scholtz, J.M.2    Pace, C.N.3
  • 24
    • 1642559369 scopus 로고    scopus 로고
    • Crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor
    • Norman R.A., Barry S.T., Bate M., Breed J., Colls J.G., Ernill R.J., et al. Crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor. Structure 12 (2004) 75-84
    • (2004) Structure , vol.12 , pp. 75-84
    • Norman, R.A.1    Barry, S.T.2    Bate, M.3    Breed, J.4    Colls, J.G.5    Ernill, R.J.6
  • 25
    • 0032516763 scopus 로고    scopus 로고
    • Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase
    • Pugmire M.J., Cook W.J., Jasanoff A., Walter M.R., and Ealick S.E. Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase. J. Mol. Biol. 281 (1998) 285-299
    • (1998) J. Mol. Biol. , vol.281 , pp. 285-299
    • Pugmire, M.J.1    Cook, W.J.2    Jasanoff, A.3    Walter, M.R.4    Ealick, S.E.5
  • 26
    • 0032533446 scopus 로고    scopus 로고
    • The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation
    • Pugmire M.J., and Ealick S.E. The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation. Structure 6 (1998) 1467-1479
    • (1998) Structure , vol.6 , pp. 1467-1479
    • Pugmire, M.J.1    Ealick, S.E.2
  • 27
    • 0032548449 scopus 로고    scopus 로고
    • Kinetics and energetics of subunit dissociation/unfolding of TIM: the importance of oligomerization for conformational persistence and chemical stability of proteins
    • Rietveld A.W., and Ferreira S.T. Kinetics and energetics of subunit dissociation/unfolding of TIM: the importance of oligomerization for conformational persistence and chemical stability of proteins. Biochemistry 37 (1998) 933-937
    • (1998) Biochemistry , vol.37 , pp. 933-937
    • Rietveld, A.W.1    Ferreira, S.T.2
  • 28
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: improvement in accuracy of multiple sequence alignment
    • Katoh K., Kuma K., Toh H., and Miyata T. MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucl. Acids Res. 33 (2005) 511-518
    • (2005) Nucl. Acids Res. , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 29
    • 0034822181 scopus 로고    scopus 로고
    • Probing the role of oligomerization in the high thermal stability of Pyrococcus furiosus ornithine carbamoyltransferase by site-specific mutants
    • Clantin B., Tricot C., Lonhienne T., Stalon V., and Villeret V. Probing the role of oligomerization in the high thermal stability of Pyrococcus furiosus ornithine carbamoyltransferase by site-specific mutants. Eur. J. Biochem. 268 (2001) 3937-3942
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3937-3942
    • Clantin, B.1    Tricot, C.2    Lonhienne, T.3    Stalon, V.4    Villeret, V.5
  • 30
    • 0024565551 scopus 로고
    • Purification and characterization of yeast anthranilate phosphoribosyltransferase
    • Hommel U., Lustig A., and Kirschner K. Purification and characterization of yeast anthranilate phosphoribosyltransferase. Eur. J. Biochem. 180 (1989) 33-40
    • (1989) Eur. J. Biochem. , vol.180 , pp. 33-40
    • Hommel, U.1    Lustig, A.2    Kirschner, K.3
  • 31
    • 0017404915 scopus 로고
    • Immunochemical analysis of the anthranilate synthase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase aggregate of Escherichia coli
    • Largen M., and Mills S.E. Immunochemical analysis of the anthranilate synthase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase aggregate of Escherichia coli. Biochemistry 16 (1977) 2526-2532
    • (1977) Biochemistry , vol.16 , pp. 2526-2532
    • Largen, M.1    Mills, S.E.2
  • 32
    • 0037424668 scopus 로고    scopus 로고
    • The universal ancestor was a thermophile or a hyperthermophile: tests and further evidence
    • Di Giulio M. The universal ancestor was a thermophile or a hyperthermophile: tests and further evidence. J. Theor. Biol. 221 (2003) 425-436
    • (2003) J. Theor. Biol. , vol.221 , pp. 425-436
    • Di Giulio, M.1
  • 33
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., and Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77 (1989) 51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 34
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension
    • Horton R.M., Hunt H.D., Ho S.N., Pullen J.K., and Pease L.R. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77 (1989) 61-68
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 36
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 37
    • 33751564683 scopus 로고
    • Sedimentation equilibria of polydisperse non-ideal solutes. VI. Number-average molecular weight and molecular-weight distribution functions
    • Wales M., Adler F.T., and Van Holde K.E. Sedimentation equilibria of polydisperse non-ideal solutes. VI. Number-average molecular weight and molecular-weight distribution functions. J. Phys. Colloid Chem. 55 (1951) 145-161
    • (1951) J. Phys. Colloid Chem. , vol.55 , pp. 145-161
    • Wales, M.1    Adler, F.T.2    Van Holde, K.E.3
  • 38
    • 0001038767 scopus 로고
    • Equilibrium ultracentrifugation of dilute solutions
    • Yphantis D.A. Equilibrium ultracentrifugation of dilute solutions. Biochemistry 3 (1964) 297-317
    • (1964) Biochemistry , vol.3 , pp. 297-317
    • Yphantis, D.A.1
  • 39
    • 0025255092 scopus 로고
    • Buffers: principles and practice
    • Stoll V.S., and Blanchard J.S. Buffers: principles and practice. Methods Enzymol. 182 (1990) 24-38
    • (1990) Methods Enzymol. , vol.182 , pp. 24-38
    • Stoll, V.S.1    Blanchard, J.S.2
  • 40
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 26 (1993) 795-800
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 42
    • 84889120137 scopus 로고
    • Improved methods for building 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. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A 47 (1991) 110-119
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 43
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 45
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., and Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6 (1999) 458-463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.