메뉴 건너뛰기




Volumn 9, Issue 8, 2008, Pages 802-809

The nature and character of the transition state for the ADP-ribosyltransferase reaction

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ELONGATION FACTOR 2; EXOTOXIN; EXOTOXIN A; GLUTAMINE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE;

EID: 48649104853     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/embor.2008.90     Document Type: Article
Times cited : (76)

References (26)
  • 1
    • 0035337247 scopus 로고    scopus 로고
    • Application of a fluorometric assay for characterization of the catalytic competency of a domain III fragment of Pseudomonas aeruginosa exotoxin A
    • Armstrong S, Merrill AR (2001) Application of a fluorometric assay for characterization of the catalytic competency of a domain III fragment of Pseudomonas aeruginosa exotoxin A. Anal Biochem 292: 26-33
    • (2001) Anal Biochem , vol.292 , pp. 26-33
    • Armstrong, S.1    Merrill, A.R.2
  • 2
    • 0037195812 scopus 로고    scopus 로고
    • Insight into the catalytic mechanism of Pseudomonas aeruginosa exotoxin A. Studies of toxin interaction with eukaryotic elongation factor-2
    • Armstrong S, Yates SP, Merrill AR (2002) Insight into the catalytic mechanism of Pseudomonas aeruginosa exotoxin A. Studies of toxin interaction with eukaryotic elongation factor-2. J Biol Chem 277: 46669-46675
    • (2002) J Biol Chem , vol.277 , pp. 46669-46675
    • Armstrong, S.1    Yates, S.P.2    Merrill, A.R.3
  • 3
    • 0029856407 scopus 로고    scopus 로고
    • Investigation into the catalytic role for the tryptophan residues within domain III of Pseudomonas aeruginosa exotoxin A
    • Beattie BK, Prentice GA, Merrill AR (1996) Investigation into the catalytic role for the tryptophan residues within domain III of Pseudomonas aeruginosa exotoxin A. Biochemistry 35: 15134-15142
    • (1996) Biochemistry , vol.35 , pp. 15134-15142
    • Beattie, B.K.1    Prentice, G.A.2    Merrill, A.R.3
  • 4
    • 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
  • 5
    • 0037881920 scopus 로고    scopus 로고
    • Functional aspects of protein mono-ADP-ribosylation
    • Corda D, Di Girolamo M (2003) Functional aspects of protein mono-ADP-ribosylation. EMBO J 122: 1953-1958
    • (2003) EMBO J , vol.122 , pp. 1953-1958
    • Corda, D.1    Di Girolamo, M.2
  • 7
    • 0036196923 scopus 로고    scopus 로고
    • The ARTT motif and a unified structural understanding of substrate recognition in ADP-ribosylating bacterial toxins and eukaryotic ADP-ribosyltransferases
    • Han S, Tainer JA (2002) The ARTT motif and a unified structural understanding of substrate recognition in ADP-ribosylating bacterial toxins and eukaryotic ADP-ribosyltransferases. Int J Med Microbiol 291: 523-529
    • (2002) Int J Med Microbiol , vol.291 , pp. 523-529
    • Han, S.1    Tainer, J.A.2
  • 8
    • 0032876380 scopus 로고    scopus 로고
    • Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex
    • Han S, Craig JA, Putnam CD, Carozzi NB, Tainer JA (1999) Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex. Nat Struct Biol 6: 932-936
    • (1999) Nat Struct Biol , vol.6 , pp. 932-936
    • Han, S.1    Craig, J.A.2    Putnam, C.D.3    Carozzi, N.B.4    Tainer, J.A.5
  • 9
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr A 47: 110-119
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 14
    • 0029075884 scopus 로고
    • The crystal structure of Pseudomonas aeruginosa exotoxin domain III with nicotinamide and AMP: Conformational differences with the intact exotoxin
    • Li M, Dyda F, Benhar I, Pastan I, Davies DR (1995) The crystal structure of Pseudomonas aeruginosa exotoxin domain III with nicotinamide and AMP: Conformational differences with the intact exotoxin. Proc Natl Acad Sci USA 92: 9308-9312
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9308-9312
    • Li, M.1    Dyda, F.2    Benhar, I.3    Pastan, I.4    Davies, D.R.5
  • 15
    • 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
  • 17
    • 23644438026 scopus 로고    scopus 로고
    • Structural basis for the activation of cholera toxin by human ARF6-GTP
    • O'Neal CJ, Jobling MG, Holmes RK, Hol WG (2005) Structural basis for the activation of cholera toxin by human ARF6-GTP. Science 309: 1093-1096
    • (2005) Science , vol.309 , pp. 1093-1096
    • O'Neal, C.J.1    Jobling, M.G.2    Holmes, R.K.3    Hol, W.G.4
  • 18
    • 0842348742 scopus 로고    scopus 로고
    • Transition state structure for ADP-ribosylation of eukaryotic elongation factor 2 catalyzed by diphtheria toxin
    • Parikh SL, Schramm VL (2004) Transition state structure for ADP-ribosylation of eukaryotic elongation factor 2 catalyzed by diphtheria toxin. Biochemistry 43: 1204-1212
    • (2004) Biochemistry , vol.43 , pp. 1204-1212
    • Parikh, S.L.1    Schramm, V.L.2
  • 19
    • 16544378761 scopus 로고    scopus 로고
    • Bacterial exotoxins
    • Popoff MR (2005) Bacterial exotoxins. Contrib Microbiol 12: 28-54
    • (2005) Contrib Microbiol , vol.12 , pp. 28-54
    • Popoff, M.R.1
  • 21
    • 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
  • 23
    • 0026609066 scopus 로고
    • Diphtheria toxin and Pseudomonas aeruginosa exotoxin A: Active-site structure and enzymic mechanism
    • Wilson BA, Collier RI (1992) Diphtheria toxin and Pseudomonas aeruginosa exotoxin A: Active-site structure and enzymic mechanism. Curr Top Microbiol Immunol 175: 27-41
    • (1992) Curr Top Microbiol Immunol , vol.175 , pp. 27-41
    • Wilson, B.A.1    Collier, R.I.2
  • 24
    • 2542526100 scopus 로고    scopus 로고
    • Elucidation of eukaryotic elongation factor-2 contact sites within the catalytic domain of Pseudomonas aeruginosa exotoxin A
    • Yates SP, Merrill AR (2004) Elucidation of eukaryotic elongation factor-2 contact sites within the catalytic domain of Pseudomonas aeruginosa exotoxin A. Biochem J 379: 563-572
    • (2004) Biochem J , vol.379 , pp. 563-572
    • Yates, S.P.1    Merrill, A.R.2
  • 25
    • 13444274564 scopus 로고    scopus 로고
    • Structure-function analysis of water-soluble inhibitors of the catalytic domain of exotoxin A from Pseudomonas aeruginosa
    • Yates SP, Taylor PL, Jorgensen R, Ferraris D, Zhang J, Andersen GR, Merrill AR (2005) Structure-function analysis of water-soluble inhibitors of the catalytic domain of exotoxin A from Pseudomonas aeruginosa. Biochem J 385: 667-675
    • (2005) Biochem J , vol.385 , pp. 667-675
    • Yates, S.P.1    Taylor, P.L.2    Jorgensen, R.3    Ferraris, D.4    Zhang, J.5    Andersen, G.R.6    Merrill, A.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.