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Volumn 274, Issue 16, 2007, Pages 4315-4325

Crystal structure of archaeal highly thermostable L-aspartate dehydrogenase/NAD/citrate ternary complex

Author keywords

Aromatic pair interaction; Hyperthermostable L aspartate dehydrogenase; Ion pair interaction; NAD biosynthesis

Indexed keywords

ARCHAEAL PROTEIN; ASPARTIC ACID; CITRIC ACID; L ASPARTATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PROTEIN SUBUNIT; TERNARY COMPLEX FACTOR; UNCLASSIFIED DRUG;

EID: 34547798477     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05961.x     Document Type: Article
Times cited : (13)

References (35)
  • 1
    • 0019921265 scopus 로고
    • The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is d-aspartate oxidase
    • Nasu S, Wicks FD Gholson RK (1982) The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is d-aspartate oxidase. Biochim Biophys Acta 704, 240 252.
    • (1982) Biochim Biophys Acta , vol.704 , pp. 240-252
    • Nasu, S.1    Wicks, F.D.2    Gholson, R.K.3
  • 2
    • 0036918074 scopus 로고    scopus 로고
    • Structural biology of enzymes involved in NAD and molybdenum cofactor biosynthesis
    • Rizzi M Schindelin H (2002) Structural biology of enzymes involved in NAD and molybdenum cofactor biosynthesis. Curr Opin Struct Biol 12, 709 720.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 709-720
    • Rizzi, M.1    Schindelin, H.2
  • 3
    • 0036688941 scopus 로고    scopus 로고
    • L-Aspartate oxidase is present in the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii OT-3: Characteristics and role in the de novo biosynthesis of nicotinamide adenine dinucleotide proposed by genome sequencing
    • Sakuraba H, Satomura T, Kawakami R, Yamamoto S, Kawarabayasi Y, Kikuchi H Ohshima T (2002) l-Aspartate oxidase is present in the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii OT-3: characteristics and role in the de novo biosynthesis of nicotinamide adenine dinucleotide proposed by genome sequencing. Extremophiles 6, 275 281.
    • (2002) Extremophiles , vol.6 , pp. 275-281
    • Sakuraba, H.1    Satomura, T.2    Kawakami, R.3    Yamamoto, S.4    Kawarabayasi, Y.5    Kikuchi, H.6    Ohshima, T.7
  • 4
    • 0037424378 scopus 로고    scopus 로고
    • Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643
    • Yang Z, Savchenko A, Yakunin A, Zhang R, Edwards A, Arrowsmith C Tong L (2003) Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643. J Biol Chem 278, 8804 8808.
    • (2003) J Biol Chem , vol.278 , pp. 8804-8808
    • Yang, Z.1    Savchenko, A.2    Yakunin, A.3    Zhang, R.4    Edwards, A.5    Arrowsmith, C.6    Tong, L.7
  • 5
    • 33745218027 scopus 로고    scopus 로고
    • The first archaeal l-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: Gene cloning and enzymological characterization
    • Yoneda K, Kawakami R, Tagashira Y, Sakuraba H, Goda S Ohshima T (2006) The first archaeal l-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: gene cloning and enzymological characterization. Biochim Biophys Acta 1764, 1087 1093.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1087-1093
    • Yoneda, K.1    Kawakami, R.2    Tagashira, Y.3    Sakuraba, H.4    Goda, S.5    Ohshima, T.6
  • 6
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW (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
  • 7
    • 0026685776 scopus 로고
    • Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold. Implications for nucleotide specificity
    • Baker PJ, Britton KL, Rice DW, Rob A Stillman TJ (1992) Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold. Implications for nucleotide specificity. J Mol Biol 228, 662 671.
    • (1992) J Mol Biol , vol.228 , pp. 662-671
    • Baker, P.J.1    Britton, K.L.2    Rice, D.W.3    Rob, A.4    Stillman, T.J.5
  • 8
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • Scrutton NS, Berry A Perham RN (1990) Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature 343, 38 43.
    • (1990) Nature , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 9
    • 0025191073 scopus 로고
    • A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzyme
    • Feeney R, Clarke AR Holbrook JJ (1990) A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzyme. Biochem Biophys Res Commun 166, 667 672.
    • (1990) Biochem Biophys Res Commun , vol.166 , pp. 667-672
    • Feeney, R.1    Clarke, A.R.2    Holbrook, J.J.3
  • 10
    • 0025989616 scopus 로고
    • Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase
    • Chen Z, Lee WR Chang SH (1991) Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase. Eur J Biochem 202, 263 267.
    • (1991) Eur J Biochem , vol.202 , pp. 263-267
    • Chen, Z.1    Lee, W.R.2    Chang, S.H.3
  • 11
    • 0025867105 scopus 로고
    • An aspartate residue in yeast alcohol dehydrogenase I determines the specificity for coenzyme
    • Fan F, Lorenzen JA Plapp BV (1991) An aspartate residue in yeast alcohol dehydrogenase I determines the specificity for coenzyme. Biochemistry 30, 6397 6401.
    • (1991) Biochemistry , vol.30 , pp. 6397-6401
    • Fan, F.1    Lorenzen, J.A.2    Plapp, B.V.3
  • 12
    • 0027415645 scopus 로고
    • Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis
    • Nishiyama M, Birktoft JJ Beppu T (1993) Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis. J Biol Chem 268, 4656 4660.
    • (1993) J Biol Chem , vol.268 , pp. 4656-4660
    • Nishiyama, M.1    Birktoft, J.J.2    Beppu, T.3
  • 13
    • 0031846232 scopus 로고    scopus 로고
    • Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase
    • Baker PJ, Sawa Y, Shibata H, Sedelnikova SE Rice DW (1998) Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase. Nat Struct Biol 5, 561 567.
    • (1998) Nat Struct Biol , vol.5 , pp. 561-567
    • Baker, P.J.1    Sawa, Y.2    Shibata, H.3    Sedelnikova, S.E.4    Rice, D.W.5
  • 14
    • 33845318295 scopus 로고
    • Interaction of pyrophosphate moieties with α-helixes in dinucleotide-binding proteins
    • Wierenga RK, de Maeyer MCH Hol WGJ (1985) Interaction of pyrophosphate moieties with α-helixes in dinucleotide-binding proteins. Biochemistry 24, 1346 1357.
    • (1985) Biochemistry , vol.24 , pp. 1346-1357
    • Wierenga, R.K.1    De Maeyer, M.C.H.2    Hol, W.G.J.3
  • 15
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • Chan MK, Mukund S, Kletzin A, Adams MW Rees DC (1995) Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267, 1463 1469.
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kletzin, A.3    Adams, M.W.4    Rees, D.C.5
  • 16
    • 0025996871 scopus 로고
    • Proline in α-helix: Stability and conformation studied by dynamics simulation
    • Yun RH, Anderson A Hermans J (1991) Proline in α-helix: stability and conformation studied by dynamics simulation. Proteins 10, 219 228.
    • (1991) Proteins , vol.10 , pp. 219-228
    • Yun, R.H.1    Anderson, A.2    Hermans, J.3
  • 18
    • 0031686238 scopus 로고    scopus 로고
    • Helix-stabilizing factors and stabilization of thermophilic proteins: An X-ray based study
    • Facchiano AM, Colonna G Ragone R (1998) Helix-stabilizing factors and stabilization of thermophilic proteins: an X-ray based study. Protein Eng 11, 753 760.
    • (1998) Protein Eng , vol.11 , pp. 753-760
    • Facchiano, A.M.1    Colonna, G.2    Ragone, R.3
  • 19
    • 0028994307 scopus 로고
    • 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability
    • Hennig M, Darimont B, Sterner R, Kirschner K Jansonius JN (1995) 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structure 3, 1295 1306.
    • (1995) Structure , vol.3 , pp. 1295-1306
    • Hennig, M.1    Darimont, B.2    Sterner, R.3    Kirschner, K.4    Jansonius, J.N.5
  • 21
    • 0030748521 scopus 로고    scopus 로고
    • The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 Å resolution: Structural basis for thermostability
    • Lim JH, Yu YG, Han YS, Cho S, Ahn BY, Kim SH Cho Y (1997) The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 Å resolution: structural basis for thermostability. J Mol Biol 270, 259 274.
    • (1997) J Mol Biol , vol.270 , pp. 259-274
    • Lim, J.H.1    Yu, Y.G.2    Han, Y.S.3    Cho, S.4    Ahn, B.Y.5    Kim, S.H.6    Cho, Y.7
  • 22
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • Burley SK Petsko GA (1985) Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science 229, 23 28.
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 23
    • 0034495733 scopus 로고    scopus 로고
    • Aromatic clusters: A determinant of thermal stability of thermophilic proteins
    • Kannan N Vishveshwara S (2000) Aromatic clusters: a determinant of thermal stability of thermophilic proteins. Protein Eng 13, 753 761.
    • (2000) Protein Eng , vol.13 , pp. 753-761
    • Kannan, N.1    Vishveshwara, S.2
  • 24
    • 0025756736 scopus 로고
    • Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles
    • Serrano L, Bycroft M Fersht AR (1991) Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles. J Mol Biol 218, 465 475.
    • (1991) J Mol Biol , vol.218 , pp. 465-475
    • Serrano, L.1    Bycroft, M.2    Fersht, A.R.3
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z 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
  • 26
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger TC Berendzen J (1999) Automated MAD and MIR structure solution. Acta Crystallogr D55, 849 861.
    • (1999) Acta Crystallogr , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 27
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger TC (2000) Maximum-likelihood density modification. Acta Crystallogr D56, 965 972.
    • (2000) Acta Crystallogr , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 28
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee DE (1999) XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density. J Struct Biol 125, 156 165.
    • (1999) J Struct Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 29
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D53, 240 255.
    • (1997) Acta Crystallogr , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 32
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model and software evaluation: Three related resources
    • Rodriguez R, Chinea G, Lopez N, Pons T Vriend G (1998) Homology modeling, model and software evaluation: three related resources. Bioinformatics 14, 523 528.
    • (1998) Bioinformatics , vol.14 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 34
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA Honig B (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281 296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 35
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22, 4673 4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.