메뉴 건너뛰기




Volumn 6, Issue 10, 1997, Pages 2084-2096

Unusual conformation of nicotinamide adenine dinucleotide (NAD) bound to diphtheria toxin: A comparison with NAD bound to the oxidoreductase enzymes

Author keywords

Diphtheria toxin; NAD conformation; Nicotinamide adenine dinucleotide (NAD); Principal component analysis; Rossmann fold; Structural Classification of Proteins (SCOP) database

Indexed keywords

DIPHTHERIA TOXIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE;

EID: 0030807274     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560061004     Document Type: Article
Times cited : (64)

References (42)
  • 1
    • 0028773899 scopus 로고
    • Crystallographic study of coenzyme, coenzyme analogue, and substrate binding in 6-phosphogluconate dehydrogenase: Implications for NADP specificity and the enzyme mechanism
    • Adams MJ, Ellis GH, Gover S, Naylor CE, Phillips C. 1994. Crystallographic study of coenzyme, coenzyme analogue, and substrate binding in 6-phosphogluconate dehydrogenase: Implications for NADP specificity and the enzyme mechanism. Structure (Lond) 2:651-668.
    • (1994) Structure (Lond) , vol.2 , pp. 651-668
    • Adams, M.J.1    Ellis, G.H.2    Gover, S.3    Naylor, C.E.4    Phillips, C.5
  • 2
    • 0030031666 scopus 로고    scopus 로고
    • Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide
    • Bell CE, Eisenberg D. 1996. Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide. Biochemistry 35:1137-1149.
    • (1996) Biochemistry , vol.35 , pp. 1137-1149
    • Bell, C.E.1    Eisenberg, D.2
  • 3
    • 0018882702 scopus 로고
    • Structure and mechanism of liver alcohol dehydrogenase, lactate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase
    • Jeffery J, ed. Basel: Birkhauser Verlag
    • Branden CI, Eklund H. 1980. Structure and mechanism of liver alcohol dehydrogenase, lactate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase. In: Jeffery J, ed. Dehydrogenases requiring nicotinamide coenzymes. Basel: Birkhauser Verlag. pp 40-84.
    • (1980) Dehydrogenases Requiring Nicotinamide Coenzymes , pp. 40-84
    • Branden, C.I.1    Eklund, H.2
  • 5
    • 0016609883 scopus 로고
    • Diphtheria toxin: Mode of action and structure
    • Collier RJ. 1975. Diphtheria toxin: Mode of action and structure. Bacteriol Rev 39:54-85.
    • (1975) Bacteriol Rev , vol.39 , pp. 54-85
    • Collier, R.J.1
  • 6
    • 0028988237 scopus 로고
    • Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis
    • Dessen A, Quemard A, Blanchard JS, Jacobs WR Jr, Sacchettini JC. 1995. Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis. Science 267:1638-41.
    • (1995) Science , vol.267 , pp. 1638-1641
    • Dessen, A.1    Quemard, A.2    Blanchard, J.S.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 7
    • 0015994218 scopus 로고
    • Real-space refinement of the structure of hen egg-white lysozyme
    • Diamond R. 1974. Real-space refinement of the structure of hen egg-white lysozyme. J Mol Biol 82:371-391.
    • (1974) J Mol Biol , vol.82 , pp. 371-391
    • Diamond, R.1
  • 8
    • 0038058016 scopus 로고    scopus 로고
    • Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dchydrogenases: Implication for NAD binding and cooperativity
    • Duee E, Olivier-Deyris L, Fanchon E, Corbier C, Branlant G, Dideberg O. 1996. Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dchydrogenases: Implication for NAD binding and cooperativity. J Mol Biol 257:814-38.
    • (1996) J Mol Biol , vol.257 , pp. 814-838
    • Duee, E.1    Olivier-Deyris, L.2    Fanchon, E.3    Corbier, C.4    Branlant, G.5    Dideberg, O.6
  • 9
    • 0001890332 scopus 로고
    • Crystal structure, coenzyme conformations, and protein interactions
    • Dolphin DNY, ed. New York: Wiley
    • Eklund H, Branden CI. 1987. Crystal structure, coenzyme conformations, and protein interactions. In: Dolphin DNY, ed. Pyridine nucleotide coenzymes. New York: Wiley. pp 51-98.
    • (1987) Pyridine Nucleotide Coenzymes , pp. 51-98
    • Eklund, H.1    Branden, C.I.2
  • 10
    • 0021701199 scopus 로고
    • Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase
    • Eklund H, Samama JP, Jones TA. 1984. Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase. Biochemistry 23:5982-5996.
    • (1984) Biochemistry , vol.23 , pp. 5982-5996
    • Eklund, H.1    Samama, J.P.2    Jones, T.A.3
  • 11
    • 0345345539 scopus 로고
    • The NADPH binding site on beef liver catalase
    • Fita I, Rossmann MG. 1985. The NADPH binding site on beef liver catalase. Proc Natl Acad Sci USA 82:1604.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 1604
    • Fita, I.1    Rossmann, M.G.2
  • 12
    • 0028773893 scopus 로고
    • The refined three-dimensional structure of 3-α,20-β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases
    • Ghosh D, Wawrzak Z, Weeks CM, Duax WL, Erman M. 1994. The refined three-dimensional structure of 3-α,20-β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases. Structure 2:629-40.
    • (1994) Structure , vol.2 , pp. 629-640
    • Ghosh, D.1    Wawrzak, Z.2    Weeks, C.M.3    Duax, W.L.4    Erman, M.5
  • 13
    • 0029001848 scopus 로고
    • Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH
    • Gouet P, Jouve HM, Dideberg O. 1995. Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH. J Mol Biol 249:933-954.
    • (1995) J Mol Biol , vol.249 , pp. 933-954
    • Gouet, P.1    Jouve, H.M.2    Dideberg, O.3
  • 14
    • 0002277561 scopus 로고
    • Structural interactions with enzymes
    • Everse J, Anderson B, You KS, eds. New York: Academic Press
    • Grau UM. 1982. Structural interactions with enzymes. In: Everse J, Anderson B, You KS, eds. The pyridine nucleotide coenzymes. New York: Academic Press. pp 135-187.
    • (1982) The Pyridine Nucleotide Coenzymes , pp. 135-187
    • Grau, U.M.1
  • 15
    • 0028774536 scopus 로고
    • Structure of 3-isopropylmalate dehydrogenase in complex with NAD+: Ligand-induced loop closing and mechanism for cofactor specificity
    • Hurley JH, Dean AM. 1994. Structure of 3-isopropylmalate dehydrogenase in complex with NAD+: Ligand-induced loop closing and mechanism for cofactor specificity. Structure 2:1007-1016.
    • (1994) Structure , vol.2 , pp. 1007-1016
    • Hurley, J.H.1    Dean, A.M.2
  • 16
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones TA. 1978. A graphics model building and refinement system for macromolecules. J Appl Crystallogr 11:268-272.
    • (1978) J Appl Crystallogr , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 17
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. 1976. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr A 32:922-923.
    • (1976) Acta Crystallogr A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 18
    • 0027156651 scopus 로고
    • Determinants of protein thermostability observed in the 1.9 Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus
    • Kelly CA, Nishiyama M, Ohnishi Y, Beppu T, Birktoft JJ. 1993. Determinants of protein thermostability observed in the 1.9 Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus. Biochemistry 32:3913-3922.
    • (1993) Biochemistry , vol.32 , pp. 3913-3922
    • Kelly, C.A.1    Nishiyama, M.2    Ohnishi, Y.3    Beppu, T.4    Birktoft, J.J.5
  • 19
    • 0024421234 scopus 로고
    • Substrate binding and catalysis by glutathione reductase as derived from refined enzyme:Substrate crystal structures at 2.0 Å resolution
    • Karplus PA, Schulz GE. 1989. Substrate binding and catalysis by glutathione reductase as derived from refined enzyme:substrate crystal structures at 2.0 Å resolution. J Mol Biol 210:163-180.
    • (1989) J Mol Biol , vol.210 , pp. 163-180
    • Karplus, P.A.1    Schulz, G.E.2
  • 20
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 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
  • 22
    • 0030015488 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of Pseudomonas exotoxin A complexed with a nicotinamide adenine dinucleotide analog: Implications for the activation process and for ADP ribosylation
    • Li M, Dyda F, Benhar I, Pastan I, Davies DR. 1996. Crystal structure of the catalytic domain of Pseudomonas exotoxin A complexed with a nicotinamide adenine dinucleotide analog: Implications for the activation process and for ADP ribosylation. Proc Natl Acad Sci USA 93:6902-6906.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6902-6906
    • Li, M.1    Dyda, F.2    Benhar, I.3    Pastan, I.4    Davies, D.R.5
  • 23
    • 0015217254 scopus 로고
    • Stereochemistry of nucleic acids and their constituents. XV. Crystal and molecular structure of 2-thiocytidine dihydrate, a minor constituent of transfer ribonucleic acids
    • Lin GHY, Sundaralingam M, Arora SK. 1971. Stereochemistry of nucleic acids and their constituents. XV. Crystal and molecular structure of 2-thiocytidine dihydrate, a minor constituent of transfer ribonucleic acids. J Am Chem Soc 93:1235-1241.
    • (1971) J Am Chem Soc , vol.93 , pp. 1235-1241
    • Lin, G.H.Y.1    Sundaralingam, M.2    Arora, S.K.3
  • 24
    • 0016772409 scopus 로고
    • Analysis of N-glycosyl bond length in crystal structures of nucleosides and nucleotides
    • Lo A, Shefter E, Cochran TG. 1975. Analysis of N-glycosyl bond length in crystal structures of nucleosides and nucleotides. J Pharm Sci 64:1707-1710.
    • (1975) J Pharm Sci , vol.64 , pp. 1707-1710
    • Lo, A.1    Shefter, E.2    Cochran, T.G.3
  • 25
    • 0019297051 scopus 로고
    • Ligand interactions of diphtheria toxin I. Binding and hydrolysis of NAD
    • Lory S, Carroll SF, Bernard PD, Collier RJ. 1980. Ligand interactions of diphtheria toxin I. Binding and hydrolysis of NAD. J Biol Chem 255:12011-12015.
    • (1980) J Biol Chem , vol.255 , pp. 12011-12015
    • Lory, S.1    Carroll, S.F.2    Bernard, P.D.3    Collier, R.J.4
  • 26
    • 0026696413 scopus 로고
    • The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 Å resolution
    • Mattevi A, Obmoloua G, Sokatch JR, Betzel C, Hol WGJ. 1992. The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 Å resolution. Proteins Struct Funct Genet 13:36-351.
    • (1992) Proteins Struct Funct Genet , vol.13 , pp. 36-351
    • Mattevi, A.1    Obmoloua, G.2    Sokatch, J.R.3    Betzel, C.4    Hol, W.G.J.5
  • 27
    • 0027294814 scopus 로고
    • A study into the effects of protein binding on nucleotide conformation
    • Moodie SL, Thornton JM. 1993. A study into the effects of protein binding on nucleotide conformation. Nucleic Acids Res 21:1369-1380.
    • (1993) Nucleic Acids Res , vol.21 , pp. 1369-1380
    • Moodie, S.L.1    Thornton, J.M.2
  • 28
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structure
    • Murzin AG, Brenner SE, Hubbard T, Chothia C. 1995. SCOP: A structural classification of proteins database for the investigation of sequences and structure. J Mol Biol 247:536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 29
    • 0029113652 scopus 로고
    • Crystal structure of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus at 2.2 Å resolution. An example of strong asymmetry between subunits
    • Niefind K, Hecht HJ, Schomberg D. 1995. Crystal structure of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus at 2.2 Å resolution. An example of strong asymmetry between subunits. J Mol Biol 251:256-281.
    • (1995) J Mol Biol , vol.251 , pp. 256-281
    • Niefind, K.1    Hecht, H.J.2    Schomberg, D.3
  • 32
    • 0028937651 scopus 로고
    • Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase
    • Scapin G, Blanchard JS, Sacchettini JC. 1995. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. Biochemistry 34:3502-3512.
    • (1995) Biochemistry , vol.34 , pp. 3502-3512
    • Scapin, G.1    Blanchard, J.S.2    Sacchettini, J.C.3
  • 33
    • 0028951187 scopus 로고
    • The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase
    • Schuller DJ, Grant GA, Banaszak LJ. 1995. The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Nature Struct Biol 2:69-76.
    • (1995) Nature Struct Biol , vol.2 , pp. 69-76
    • Schuller, D.J.1    Grant, G.A.2    Banaszak, L.J.3
  • 34
    • 0027535570 scopus 로고
    • NADH binding site and catalysis of NAD peroxidase
    • Stehle T, Claiborne A, Schulz GE. 1993. NADH binding site and catalysis of NAD peroxidase. Eur J Biochem 211:221.
    • (1993) Eur J Biochem , vol.211 , pp. 221
    • Stehle, T.1    Claiborne, A.2    Schulz, G.E.3
  • 35
    • 0027494760 scopus 로고
    • Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5 Å resolution: A pseudo-Michaelis ternary complex
    • Stoddard BL, Dean A, Koshland DE Jr. 1993. Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5 Å resolution: a pseudo-Michaelis ternary complex. Biochemistry 32:9310-9316.
    • (1993) Biochemistry , vol.32 , pp. 9310-9316
    • Stoddard, B.L.1    Dean, A.2    Koshland Jr., D.E.3
  • 36
    • 0028977970 scopus 로고
    • Crystal structure of Escherichia coli quinone oxidoreductase complexed with NADPH
    • Thorn JM, Barton JD, Dixon NE, Ollie DL, Edwards KJ. 1995. Crystal structure of Escherichia coli quinone oxidoreductase complexed with NADPH. J Mol Biol 249:785-799.
    • (1995) J Mol Biol , vol.249 , pp. 785-799
    • Thorn, J.M.1    Barton, J.D.2    Dixon, N.E.3    Ollie, D.L.4    Edwards, K.J.5
  • 37
    • 0019333178 scopus 로고
    • ADP-ribosylation of elongation factor 2 by diphtheria toxin. NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products
    • Van Ness BG, Howard JB, Bodley JW. 1980. ADP-ribosylation of elongation factor 2 by diphtheria toxin. NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products. J Biol Chem 255:10710-10716.
    • (1980) J Biol Chem , vol.255 , pp. 10710-10716
    • Van Ness, B.G.1    Howard, J.B.2    Bodley, J.W.3
  • 39
    • 0028220312 scopus 로고
    • Crystal structure of Escherichia coli thioredoxin reductase refined at 2 Å resolution. Implications for a large conformational change during catalysis
    • Waksman G, Krishna TS, Williams CH Jr, Kuriyan J. 1994. Crystal structure of Escherichia coli thioredoxin reductase refined at 2 Å resolution. Implications for a large conformational change during catalysis. J Mol Biol 236:800-816.
    • (1994) J Mol Biol , vol.236 , pp. 800-816
    • Waksman, G.1    Krishna, T.S.2    Williams Jr., C.H.3    Kuriyan, J.4
  • 40
    • 0015762525 scopus 로고
    • Conformation of nicotinamide adenine dinucleotide bound to cytoplasmic malate dehydrogenase
    • Webb LE, Hill EJ, Banaszak LJ. 1973. Conformation of nicotinamide adenine dinucleotide bound to cytoplasmic malate dehydrogenase. Biochemistry 12:5101-5109.
    • (1973) Biochemistry , vol.12 , pp. 5101-5109
    • Webb, L.E.1    Hill, E.J.2    Banaszak, L.J.3
  • 41
    • 0025076421 scopus 로고
    • Active-site mutations of diphtheria toxin: Effects of replacing glutamic acid-148 with aspartic acid, glutamine, or serine
    • Wilson BA, Reich KA, Weinstein BR, Collier RJ. 1990. Active-site mutations of diphtheria toxin: Effects of replacing glutamic acid-148 with aspartic acid, glutamine, or serine. Biochemistry 29:8643-8651.
    • (1990) Biochemistry , vol.29 , pp. 8643-8651
    • Wilson, B.A.1    Reich, K.A.2    Weinstein, B.R.3    Collier, R.J.4
  • 42
    • 0026719692 scopus 로고
    • An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications
    • Wilson DK, Bohren KM, Gabbay KH, Quiocho FA. 1992. An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257:81-84.
    • (1992) Science , vol.257 , pp. 81-84
    • Wilson, D.K.1    Bohren, K.M.2    Gabbay, K.H.3    Quiocho, F.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.