메뉴 건너뛰기




Volumn 366, Issue 3, 2007, Pages 857-867

The First Crystal Structure of l-Threonine Dehydrogenase

Author keywords

alcohol dehydrogenase; archaea; Pyrococcus horikoshii; threonine dehydrogenase; X ray crystallography

Indexed keywords

2 AMINO 3 KETOBUTYRATE; ALCOHOL DEHYDROGENASE; BINDING PROTEIN; BUTYRIC ACID DERIVATIVE; NICOTINAMIDE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SELENOMETHIONINE; THREONINE; THREONINE 3 DEHYDROGENASE; UNCLASSIFIED DRUG; ZINC ION;

EID: 33846604529     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.11.060     Document Type: Article
Times cited : (33)

References (41)
  • 1
    • 2642641281 scopus 로고    scopus 로고
    • Pyrococcus horikoshii sp. nov., a hyperthermophilic archaeon isolated from a hydrothermal vent at the Okinawa Trough
    • Gonzalez J.M., Masuchi Y., Robb F.T., Ammerman J.W., Maeder D.L., and Yanagibayashi M. Pyrococcus horikoshii sp. nov., a hyperthermophilic archaeon isolated from a hydrothermal vent at the Okinawa Trough. Extremophiles 2 (1998) 123-130
    • (1998) Extremophiles , vol.2 , pp. 123-130
    • Gonzalez, J.M.1    Masuchi, Y.2    Robb, F.T.3    Ammerman, J.W.4    Maeder, D.L.5    Yanagibayashi, M.6
  • 2
    • 0032579989 scopus 로고    scopus 로고
    • Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3
    • Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., and Yamamoto S. Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3. DNA Res. 5 (1998) 55-76
    • (1998) DNA Res. , vol.5 , pp. 55-76
    • Kawarabayasi, Y.1    Sawada, M.2    Horikawa, H.3    Haikawa, Y.4    Hino, Y.5    Yamamoto, S.6
  • 3
    • 17044438727 scopus 로고    scopus 로고
    • Kinetic study of thermostable l-threonine dehydrogenase from an archaeon Pyrococcus horikoshii
    • Higashi N., Fukada H., and Ishikawa K. Kinetic study of thermostable l-threonine dehydrogenase from an archaeon Pyrococcus horikoshii. J. Biosci. Bioeng. 99 (2005) 175-180
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 175-180
    • Higashi, N.1    Fukada, H.2    Ishikawa, K.3
  • 4
    • 0025847512 scopus 로고
    • l-Threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies
    • Epperly B.R., and Dekker E.E. l-Threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies. J. Biol. Chem. 266 (1991) 6086-6092
    • (1991) J. Biol. Chem. , vol.266 , pp. 6086-6092
    • Epperly, B.R.1    Dekker, E.E.2
  • 5
    • 0032532659 scopus 로고    scopus 로고
    • Investigation of a catalytic zinc binding site in Escherichia coli l-threonine dehydrogenase by site-directed mutagenesis of cystein-38
    • Johnson A.R., Chen Y.W., and Dekker E.E. Investigation of a catalytic zinc binding site in Escherichia coli l-threonine dehydrogenase by site-directed mutagenesis of cystein-38. Arch. Biochem. Biophys. 358 (1998) 211-221
    • (1998) Arch. Biochem. Biophys. , vol.358 , pp. 211-221
    • Johnson, A.R.1    Chen, Y.W.2    Dekker, E.E.3
  • 6
    • 0019877767 scopus 로고
    • l-Threonine dehydrogenase of chicken liver. Purification, characterization, and physiological significance
    • Aoyama Y., and Motokawa Y. l-Threonine dehydrogenase of chicken liver. Purification, characterization, and physiological significance. J. Biol. Chem. 256 (1981) 12367-12373
    • (1981) J. Biol. Chem. , vol.256 , pp. 12367-12373
    • Aoyama, Y.1    Motokawa, Y.2
  • 7
    • 0021796377 scopus 로고
    • l-Threonine dehydrogenase from goat liver. Feedback inhibition by methylglyoxal
    • Ray M., and Ray S. l-Threonine dehydrogenase from goat liver. Feedback inhibition by methylglyoxal. J. Biol. Chem. 260 (1985) 5913-5918
    • (1985) J. Biol. Chem. , vol.260 , pp. 5913-5918
    • Ray, M.1    Ray, S.2
  • 8
    • 0024523884 scopus 로고
    • The primary structure of Escherichia coli l-threonine dehydrogenase
    • Aronson B.D., Somerville R.L., Epperly B.R., and Dekker E.E. The primary structure of Escherichia coli l-threonine dehydrogenase. J. Mol. Biol. 264 (1989) 5226-5232
    • (1989) J. Mol. Biol. , vol.264 , pp. 5226-5232
    • Aronson, B.D.1    Somerville, R.L.2    Epperly, B.R.3    Dekker, E.E.4
  • 9
    • 0028212644 scopus 로고
    • Molecular characterization of microbial alcohol dehydrogenases
    • Reid M.F., and Fewson C.A. Molecular characterization of microbial alcohol dehydrogenases. Crit. Rev. Microbiol. 20 (1994) 13-56
    • (1994) Crit. Rev. Microbiol. , vol.20 , pp. 13-56
    • Reid, M.F.1    Fewson, C.A.2
  • 10
    • 0036301867 scopus 로고    scopus 로고
    • Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 Å resolution
    • Esposito L., Sica F., Raia C.A., Giordano A., Rossi M., Mazzarella L., and Zagari A. Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 Å resolution. J. Mol. Biol. 318 (2002) 463-477
    • (2002) J. Mol. Biol. , vol.318 , pp. 463-477
    • Esposito, L.1    Sica, F.2    Raia, C.A.3    Giordano, A.4    Rossi, M.5    Mazzarella, L.6    Zagari, A.7
  • 11
    • 0347480310 scopus 로고    scopus 로고
    • Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus
    • Esposito L., Bruno I., Sica F., Raia C.A., Giordano A., Rossi M., et al. Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus. Biochemistry 42 (2003) 14397-14407
    • (2003) Biochemistry , vol.42 , pp. 14397-14407
    • Esposito, L.1    Bruno, I.2    Sica, F.3    Raia, C.A.4    Giordano, A.5    Rossi, M.6
  • 12
    • 0043123405 scopus 로고    scopus 로고
    • The structure of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix
    • Guy J.E., Isupov M.N., and Littlechild J.A. The structure of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix. J. Mol. Biol. 331 (2003) 1041-1051
    • (2003) J. Mol. Biol. , vol.331 , pp. 1041-1051
    • Guy, J.E.1    Isupov, M.N.2    Littlechild, J.A.3
  • 13
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublie S. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276 (1997) 523-530
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublie, S.1
  • 14
    • 33744469369 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of hyperthermophilic l-threonine dehydrogenase from archaeon Pyrococcus horikoshii
    • Higashi N., Matsuura T., Nakagawa A., and Ishikawa K. Crystallization and preliminary X-ray analysis of hyperthermophilic l-threonine dehydrogenase from archaeon Pyrococcus horikoshii. Acta Crystallog. sect. F 61 (2005) 432-434
    • (2005) Acta Crystallog. sect. F , vol.61 , pp. 432-434
    • Higashi, N.1    Matsuura, T.2    Nakagawa, A.3    Ishikawa, K.4
  • 16
    • 0016345760 scopus 로고
    • Chemical and biological evolution of nucleotide-binding protein
    • Rossmann M.G., Moras D., and Olsen K.W. Chemical and biological evolution of nucleotide-binding protein. Nature 250 (1974) 194-199
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 17
    • 0029845902 scopus 로고    scopus 로고
    • The nicontinamide dinucleotide binding motif: a comparison of nucleotide binding proteins
    • Bellamacina C.R. The nicontinamide dinucleotide binding motif: a comparison of nucleotide binding proteins. FASEB J. 11 (1996) 1257-1269
    • (1996) FASEB J. , vol.11 , pp. 1257-1269
    • Bellamacina, C.R.1
  • 18
    • 0033566181 scopus 로고    scopus 로고
    • Probing the affinity and specificity of yeast alcohol dehydrogenase I for coenzymes
    • Fan F., and Plapp B.V. Probing the affinity and specificity of yeast alcohol dehydrogenase I for coenzymes. Arch. Biochem. Biophys. 367 (1999) 240-249
    • (1999) Arch. Biochem. Biophys. , vol.367 , pp. 240-249
    • Fan, F.1    Plapp, B.V.2
  • 19
    • 0032557624 scopus 로고    scopus 로고
    • NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii
    • Korkhin Y., Kalb (Gilboa) A.J., Peretz M., Bogin O., Burstein Y., and Frolow F. NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii. J. Mol. Biol. 278 (1998) 967-981
    • (1998) J. Mol. Biol. , vol.278 , pp. 967-981
    • Korkhin, Y.1    Kalb (Gilboa), A.J.2    Peretz, M.3    Bogin, O.4    Burstein, Y.5    Frolow, F.6
  • 20
  • 21
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 22
    • 0001890332 scopus 로고
    • Clystal structure, coenzyme conformations, and protein interactions
    • Dolphin D., et al. (Ed), Wiley & Sons, New York
    • Eklund H., and Branden C.I. Clystal structure, coenzyme conformations, and protein interactions. In: Dolphin D., et al. (Ed). Pyridine Nucleotides (1987), Wiley & Sons, New York 51-98
    • (1987) Pyridine Nucleotides , pp. 51-98
    • Eklund, H.1    Branden, C.I.2
  • 23
    • 0031033967 scopus 로고    scopus 로고
    • Flexibility of liver alcohol dehydrogenase in stereoselective binding of 3-butylthiolane 1-oxides
    • Cho H., Ramaswamy S., and Plapp B.V. Flexibility of liver alcohol dehydrogenase in stereoselective binding of 3-butylthiolane 1-oxides. Biochemistry 36 (1997) 382-389
    • (1997) Biochemistry , vol.36 , pp. 382-389
    • Cho, H.1    Ramaswamy, S.2    Plapp, B.V.3
  • 24
    • 0033592324 scopus 로고    scopus 로고
    • Control of coenzyme binding to horse liver alcohol dehydrogenase
    • LeBrun L.A., and Plapp B.V. Control of coenzyme binding to horse liver alcohol dehydrogenase. Biochemistry 38 (1999) 12387-12393
    • (1999) Biochemistry , vol.38 , pp. 12387-12393
    • LeBrun, L.A.1    Plapp, B.V.2
  • 25
    • 1542743968 scopus 로고    scopus 로고
    • Participation of histidine-51 in catalysis by horse liver alcohol dehydrogenase
    • LeBrun L.A., Park D.H., Ramaswamy S., and Plapp B.V. Participation of histidine-51 in catalysis by horse liver alcohol dehydrogenase. Biochemistry 43 (2004) 3014-3026
    • (2004) Biochemistry , vol.43 , pp. 3014-3026
    • LeBrun, L.A.1    Park, D.H.2    Ramaswamy, S.3    Plapp, B.V.4
  • 26
    • 0000692015 scopus 로고
    • Zinc a component of yeast alcohol dehydrogenase
    • Vallee B.L., and Hoch F.L. Zinc a component of yeast alcohol dehydrogenase. Proc. Natl Acd. Sci. USA 41 (1955) 327-338
    • (1955) Proc. Natl Acd. Sci. USA , vol.41 , pp. 327-338
    • Vallee, B.L.1    Hoch, F.L.2
  • 27
    • 0016794138 scopus 로고
    • The intrinsic zinc atoms of yeast alcohol dehydrogenase
    • Veillon C., and Sytkwski A.J. The intrinsic zinc atoms of yeast alcohol dehydrogenase. Biochem. Biophys. Res. Commun. 67 (1975) 1494-1500
    • (1975) Biochem. Biophys. Res. Commun. , vol.67 , pp. 1494-1500
    • Veillon, C.1    Sytkwski, A.J.2
  • 28
    • 0020479867 scopus 로고
    • Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase
    • Eklund H., Plapp B.V., Samama J.P., and Branden C.I. Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase. J. Biol. Chem. 257 (1982) 14349-14358
    • (1982) J. Biol. Chem. , vol.257 , pp. 14349-14358
    • Eklund, H.1    Plapp, B.V.2    Samama, J.P.3    Branden, C.I.4
  • 29
    • 0344631780 scopus 로고    scopus 로고
    • Substitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer
    • Ramaswamy S., Park D.H., and Plapp B.V. Substitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer. Biochemistry 38 (1999) 13951-13959
    • (1999) Biochemistry , vol.38 , pp. 13951-13959
    • Ramaswamy, S.1    Park, D.H.2    Plapp, B.V.3
  • 30
    • 0028793102 scopus 로고
    • Functional analysis of E. coli threonine dehydrogenase by means of mutant isolation and characterization
    • Chen Y.W., Dekker E.E., and Somerville R.L. Functional analysis of E. coli threonine dehydrogenase by means of mutant isolation and characterization. Biochim. Biophys. Acta 1253 (1995) 208-214
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 208-214
    • Chen, Y.W.1    Dekker, E.E.2    Somerville, R.L.3
  • 31
    • 0032029788 scopus 로고    scopus 로고
    • Site-directed mutagenesisi of Histidine-90 in Escherichia coli l-threonine dehydrogenase alters its substrate specificity
    • Johnson A.R., and Dekker E.E. Site-directed mutagenesisi of Histidine-90 in Escherichia coli l-threonine dehydrogenase alters its substrate specificity. Arch. Biochem. Biophys. 351 (1998) 8-16
    • (1998) Arch. Biochem. Biophys. , vol.351 , pp. 8-16
    • Johnson, A.R.1    Dekker, E.E.2
  • 33
    • 0036445426 scopus 로고    scopus 로고
    • Crystal structure of formaldehyde dehydrogenase from Pseudomonas putida: the structural origin of the tightly bound cofactor in nicotinoprotein dehydrogenases
    • Tanaka N., Kusakabe Y., Ito K., Yoshimoto T., and Nakamura K.T. Crystal structure of formaldehyde dehydrogenase from Pseudomonas putida: the structural origin of the tightly bound cofactor in nicotinoprotein dehydrogenases. J. Mol. Biol. 324 (2002) 519-533
    • (2002) J. Mol. Biol. , vol.324 , pp. 519-533
    • Tanaka, N.1    Kusakabe, Y.2    Ito, K.3    Yoshimoto, T.4    Nakamura, K.T.5
  • 35
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: automated structure solution and density modification
    • Terwilliger T. SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol. 374 (2003) 22-37
    • (2003) Methods Enzymol. , vol.374 , pp. 22-37
    • Terwilliger, T.1
  • 36
    • 0003292939 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods
    • La Fortella E., and Bricogne G. Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods. Methods. Enzymol. 276 (1997) 472-494
    • (1997) Methods. Enzymol. , vol.276 , pp. 472-494
    • La Fortella, E.1    Bricogne, G.2
  • 37
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams J., and Leslie A. Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallog. sect. D 52 (1996) 30-42
    • (1996) Acta Crystallog. sect. D , vol.52 , pp. 30-42
    • Abrahams, J.1    Leslie, A.2
  • 38
    • 0033198415 scopus 로고    scopus 로고
    • Error estimation and bias correction in phase-improvement calculations
    • Cowtan K. Error estimation and bias correction in phase-improvement calculations. Acta Crystallog. sect. D 55 (1999) 1555-15567
    • (1999) Acta Crystallog. sect. D , vol.55 , pp. 1555-15567
    • Cowtan, K.1
  • 39
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G., Vagin A., and Dodson E. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.1    Vagin, A.2    Dodson, E.3
  • 41
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog 24 (1991) 946-959
    • (1991) J. Appl. Crystallog , vol.24 , pp. 946-959
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.