메뉴 건너뛰기




Volumn 50, Issue 1, 2003, Pages 122-134

Structural plasticity of thermophilic serine hydroxymethyltransferases

Author keywords

Archaea; Modified folates; Residue exchanges; Serine hydroxymethyltransferase; Structural adaptation; Thermophilic enzymes

Indexed keywords

GLYCINE HYDROXYMETHYLTRANSFERASE;

EID: 0037236096     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10268     Document Type: Article
Times cited : (31)

References (51)
  • 2
    • 0012606881 scopus 로고    scopus 로고
    • Extreme genomes
    • Review 1029
    • De Long R. Extreme genomes. Genome Biol 2000;1:Review 1029.
    • (2000) Genome Biol , vol.1
    • De Long, R.1
  • 3
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke R, Bohm G. The stability of proteins in extreme environments. Curr Opin Struct Biol 1998;8:738-748.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 4
    • 0011186093 scopus 로고    scopus 로고
    • Protein thermal stability: Hydrogen bonds or internal packing?
    • Vogt G, Argos P. Protein thermal stability: hydrogen bonds or internal packing? Fold Des 1997;2:540-546.
    • (1997) Fold Des , vol.2 , pp. 540-546
    • Vogt, G.1    Argos, P.2
  • 5
    • 0034855858 scopus 로고    scopus 로고
    • How do thermophilic proteins deal with heat?
    • Kumar S, Nussinov R. How do thermophilic proteins deal with heat? Cell Mol Life Sci 2001;58:1216-1233.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1216-1233
    • Kumar, S.1    Nussinov, R.2
  • 7
    • 0036568335 scopus 로고    scopus 로고
    • Comparative structural analysis ofpsychrophilic and meso- and thermophilic enzymes
    • Gianese G, Bossa F, Pascarella S. Comparative structural analysis ofpsychrophilic and meso- and thermophilic enzymes. Proteins 2002;47:236-249.
    • (2002) Proteins , vol.47 , pp. 236-249
    • Gianese, G.1    Bossa, F.2    Pascarella, S.3
  • 8
    • 0034767491 scopus 로고    scopus 로고
    • Understanding the adaptation of Halobacterium species NRC-1 to its extreme environments through computational analysis of its genome sequence
    • Kennedy SP, Ng WV, Salzberg SL, Hood L, DasSarma L. Understanding the adaptation of Halobacterium species NRC-1 to its extreme environments through computational analysis of its genome sequence. Genome Res 2001;11:1641-1650.
    • (2001) Genome Res , vol.11 , pp. 1641-1650
    • Kennedy, S.P.1    Ng, W.V.2    Salzberg, S.L.3    Hood, L.4    DasSarma, L.5
  • 9
    • 0034620588 scopus 로고    scopus 로고
    • Halophilic adaptation: Novel solvent-protein interactions observed in the 2.9 and 2.6Å resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui
    • Richard SB, Madern D, Garcin E, Zaccai G. Halophilic adaptation: novel solvent-protein interactions observed in the 2.9 and 2.6Å resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui. Biochemistry 2000; 39:992-1000.
    • (2000) Biochemistry , vol.39 , pp. 992-1000
    • Richard, S.B.1    Madern, D.2    Garcin, E.3    Zaccai, G.4
  • 10
    • 0028220701 scopus 로고
    • Proteins under pressure
    • Gross M, Jaenicke R. Proteins under pressure. Eur J Biochem 1994;221:617-630.
    • (1994) Eur J Biochem , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 12
    • 0026029043 scopus 로고
    • Distribution of folates and modified folates in extremely thermophilic bacteria
    • White RH. Distribution of folates and modified folates in extremely thermophilic bacteria. J Bacteriol 1991;173:1987-1991.
    • (1991) J Bacteriol , vol.173 , pp. 1987-1991
    • White, R.H.1
  • 13
    • 0034664991 scopus 로고    scopus 로고
    • Tetrahydrofolate and tetrahydromethanopterin compared: Functionally distinct carriers in C1 metabolism
    • Maden BEH. Tetrahydrofolate and tetrahydromethanopterin compared: functionally distinct carriers in C1 metabolism. Biochem Soc 2000;350:609-629.
    • (2000) Biochem Soc , vol.350 , pp. 609-629
    • Maden, B.E.H.1
  • 15
    • 0034731469 scopus 로고    scopus 로고
    • Approaches for deciphering the structural basis of low temperature enzyme activity
    • Sheridan PP, Panasik N, Coombs JM, Brenchley JE. Approaches for deciphering the structural basis of low temperature enzyme activity. Biochim Biophys Acta 2000;1543:417-433.
    • (2000) Biochim Biophys Acta , vol.1543 , pp. 417-433
    • Sheridan, P.P.1    Panasik, N.2    Coombs, J.M.3    Brenchley, J.E.4
  • 16
    • 0034635346 scopus 로고    scopus 로고
    • Crystal structure at 2.4Å resolution of E.coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate
    • Scarsdale JN, Radaev S, Kazanina G, Schirch V, Wright HT. Crystal structure at 2.4Å resolution of E.coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate. J Mol Biol 2000;296:155-168.
    • (2000) J Mol Biol , vol.296 , pp. 155-168
    • Scarsdale, J.N.1    Radaev, S.2    Kazanina, G.3    Schirch, V.4    Wright, H.T.5
  • 17
    • 0032530853 scopus 로고    scopus 로고
    • The crystal structure of human cytosolic serine hydroxymethyltransferase: A target for cancer chemotherapy
    • Renwick SB, Snell K, Baumann U. The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy. Structure 1998;6:1105-1116.
    • (1998) Structure , vol.6 , pp. 1105-1116
    • Renwick, S.B.1    Snell, K.2    Baumann, U.3
  • 18
    • 0033614832 scopus 로고    scopus 로고
    • Crystal structure of rabbit cytosolic serine hydroxymethyltransferase at 2.8 A resolution: Mechanistic implications
    • Scarsdale JN, Kazanina G, Radaev S, Schirch V, Wright HT. Crystal structure of rabbit cytosolic serine hydroxymethyltransferase at 2.8 A resolution: mechanistic implications. Biochemistry 1999;38:8347-8358.
    • (1999) Biochemistry , vol.38 , pp. 8347-8358
    • Scarsdale, J.N.1    Kazanina, G.2    Radaev, S.3    Schirch, V.4    Wright, H.T.5
  • 22
    • 0034489478 scopus 로고    scopus 로고
    • Evaluation of PSI-BLAST alignment accuracy in comparison to structural alignments
    • Friedberg I, Kaplan T, Margalit H. Evaluation of PSI-BLAST alignment accuracy in comparison to structural alignments. Protein Sci 2000;9:2278-2284.
    • (2000) Protein Sci , vol.9 , pp. 2278-2284
    • Friedberg, I.1    Kaplan, T.2    Margalit, H.3
  • 23
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparisons
    • Pearson WR, Lipman DJ. Improved tools for biological sequence comparisons. Proc Natl Acad Sci USA 1988;85:2444-2448.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 24
    • 0027457706 scopus 로고
    • SRS-An indexing and retrieval tool for flat file data libraries
    • Etzold T, Argos P. SRS-An indexing and retrieval tool for flat file data libraries. Comput Appl Biosci 1993;9:49-57.
    • (1993) Comput Appl Biosci , vol.9 , pp. 49-57
    • Etzold, T.1    Argos, P.2
  • 25
    • 0027968068 scopus 로고
    • CLUSTALW: Improving the sensitivity of progressive multiple alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTALW: improving the sensitivity of progressive multiple alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 26
    • 0021581577 scopus 로고
    • Distance methods for inferring phylogenies: A justification
    • Felsenstein J. Distance methods for inferring phylogenies: a justification. Evolution 1984;38:16-24.
    • (1984) Evolution , vol.38 , pp. 16-24
    • Felsenstein, J.1
  • 30
  • 31
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl MJ. Recognition of errors in three-dimensional structures of proteins. Proteins 1993;17:355-362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 32
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983;22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 33
    • 0003742069 scopus 로고
    • Department of Biochemestry and Molecular Biology, University College, London
    • Hubbard SJ, Thornton JM. NACCESS, computer program. Department of Biochemestry and Molecular Biology, University College, London, 1993.
    • (1993) NACCESS Computer Program
    • Hubbard, S.J.1    Thornton, J.M.2
  • 35
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls A, Honig B. A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation. J Comp Chem 1991;12:435-445.
    • (1991) J Comp Chem , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.2
  • 36
    • 0033616712 scopus 로고    scopus 로고
    • Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species
    • Haney PJ, Badger JH, Buldak GL, Reich CI, Woese CR, Olsen GJ. Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species. Proc Natl Acad Sci USA 1999;96:3578-3583.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3578-3583
    • Haney, P.J.1    Badger, J.H.2    Buldak, G.L.3    Reich, C.I.4    Woese, C.R.5    Olsen, G.J.6
  • 37
    • 0028091179 scopus 로고
    • Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus
    • Kirino H, Aoki M, Aoshima M, Hayashi Y, Ohba M, Yamagishi A, Wakagi T, Oshima T. Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus. Eur J Biochem 1994;220:275-281.
    • (1994) Eur J Biochem , vol.220 , pp. 275-281
    • Kirino, H.1    Aoki, M.2    Aoshima, M.3    Hayashi, Y.4    Ohba, M.5    Yamagishi, A.6    Wakagi, T.7    Oshima, T.8
  • 38
    • 0032539795 scopus 로고    scopus 로고
    • The crystal structure of Pyrococ. cus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures
    • Villeret V, Clantin B, Tricot C, Legrain C, Roovers M, Stalon V, Glansdorff N, Van Beeumen JF. The crystal structure of Pyrococ. cus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures. Proc Natl Acad Sci USA 1998;17:2801-2806.
    • (1998) Proc Natl Acad Sci USA , vol.17 , pp. 2801-2806
    • Villeret, V.1    Clantin, B.2    Tricot, C.3    Legrain, C.4    Roovers, M.5    Stalon, V.6    Glansdorff, N.7    Van Beeumen, J.F.8
  • 40
    • 0032514678 scopus 로고    scopus 로고
    • Protein thermostability above 100°C: A key role for ionic interactions
    • Vetriani C, Maeder DL, Tolliday N et al. Protein thermostability above 100°C: a key role for ionic interactions. Proc Natl Acad Sci USA 1998;95:12300-12305.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12300-12305
    • Vetriani, C.1    Maeder, D.L.2    Tolliday, N.3
  • 41
    • 0025718955 scopus 로고
    • Contributions of engineered surface to the stability of T4 lysozyme determined by directed mutagenesis
    • Sun DP, Sauer U, Nicholson H, Matthews BW. Contributions of engineered surface to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry 1991;30:7142-7153.
    • (1991) Biochemistry , vol.30 , pp. 7142-7153
    • Sun, D.P.1    Sauer, U.2    Nicholson, H.3    Matthews, B.W.4
  • 42
    • 0035448574 scopus 로고    scopus 로고
    • Ion pairs and thermotolerance of proteins from hyperthermophiles: A "traffic rule" for hot roads
    • Karshikoff A, Ladenstein R. Ion pairs and thermotolerance of proteins from hyperthermophiles: a "traffic rule" for hot roads. Trends Biochem Sci 2001;26:550-556.
    • (2001) Trends Biochem Sci , vol.26 , pp. 550-556
    • Karshikoff, A.1    Ladenstein, R.2
  • 43
    • 85047691074 scopus 로고
    • Insights into thermal stability from a comparison of the glutamate dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis
    • Britton KL, Baker PJ, Borges KMM et al. Insights into thermal stability from a comparison of the glutamate dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis. Eur J Biochem 1995;229:688-695.
    • (1995) Eur J Biochem , vol.229 , pp. 688-695
    • Britton, K.L.1    Baker, P.J.2    Borges, K.M.M.3
  • 44
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • Szilàgyi A, Zavodszky P. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. Structure 2000; 8:493-504.
    • (2000) Structure , vol.8 , pp. 493-504
    • Szilàgyi, A.1    Zavodszky, P.2
  • 46
    • 0032774370 scopus 로고    scopus 로고
    • A single domain thermophilic xylanase can bind insoluble xylan: Evidence for surface aromatic clusters
    • Connerton I, Cummings N, Harris GW, Debeire P, Breton C. A single domain thermophilic xylanase can bind insoluble xylan: evidence for surface aromatic clusters. Biochim Biophys Acta 1999;1433:110-121.
    • (1999) Biochim Biophys Acta , vol.1433 , pp. 110-121
    • Connerton, I.1    Cummings, N.2    Harris, G.W.3    Debeire, P.4    Breton, C.5
  • 47
    • 0034495733 scopus 로고    scopus 로고
    • Aromatic clusters: A determinant of thermal stability of thermophilic proteins
    • Kannan N, Vishveshwara S. Aromatic clusters: a determinant of thermal stability of thermophilic proteins. Protein Eng 2000;13: 753-761.
    • (2000) Protein Eng , vol.13 , pp. 753-761
    • Kannan, N.1    Vishveshwara, S.2
  • 48
    • 0034646311 scopus 로고    scopus 로고
    • Homology modeling, molecular dynamics simulations, and analysis of CYP119, a P450 enzyme from extreme acidothermophilic archaeon Sulfolobus solfataricus
    • Chang YT, Loew G. Homology modeling, molecular dynamics simulations, and analysis of CYP119, a P450 enzyme from extreme acidothermophilic archaeon Sulfolobus solfataricus. Biochemistry 2000;39:2484-2498.
    • (2000) Biochemistry , vol.39 , pp. 2484-2498
    • Chang, Y.T.1    Loew, G.2
  • 49
    • 0023834870 scopus 로고
    • Mechanisms of irreversible thermal inactivation of Bacillus licheniformis α-amylases
    • Tomazic SJ, Klibanov AM. Mechanisms of irreversible thermal inactivation of Bacillus licheniformis α-amylases. J Biol Chem 1988;263:3086-3091.
    • (1988) J Biol Chem , vol.263 , pp. 3086-3091
    • Tomazic, S.J.1    Klibanov, A.M.2
  • 50
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments using PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F. ESPript: analysis of multiple sequence alignments using PostScript. Bioinformatics 1999;15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.