Sequence and structural links between distant ADP-ribosyltransferase families

Advances in Experimental Medicine and Biology

Volumn 419, Issue , 1997, Pages 99-107

  Bazan, J Fernando ^a   Koch Nolte, Friedrich ^b  

^a MERCK RESEARCH LABORATORIES   (United States)

^b UNIVERSITY MEDICAL CENTER HAMBURG EPPENDORF   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; CHOLERA TOXIN; DIPHTHERIA TOXIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PERTUSSIS TOXIN; PSEUDOMONAS EXOTOXIN;

ADENOSINE DIPHOSPHATE RIBOSYLATION; BACTERIAL INFECTION; CONFERENCE PAPER; ENZYME ACTIVE SITE; ENZYME MECHANISM; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PSEUDOMONAS AERUGINOSA; TOXIN STRUCTURE;

AMINO ACID SEQUENCE; CONSERVED SEQUENCE; CYTOSINE DEAMINASE; MOLECULAR SEQUENCE DATA; NUCLEOSIDE DEAMINASES; POLY(ADP-RIBOSE) POLYMERASES; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0030920874     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper

References (38)

1. Bork, P., C. Ouzounis, C. Sander. 1994. From genome sequences to protein function. Curr. Opin. Struct. Biol. 4: 393-403.
2. Pawson, T. 1995. Protein modules and signalling networks. Nature 373: 573-580.
3. Koch-Nolte, F., F. Haag, R. Kastelein, J.F. Bazan. 1996. Uncovered - the family relationship of a T-cell membrane protein and bacterial toxins. Immunol. Today 17: 402-405.
4. Holm, L., C. Sander. 1996. Mapping the protein universe. Science 273: 595-603.
5. Fischer, D., D. Rice, J.U. Bowie, D. Eisenberg. 1996. Assigning amino acid sequences to 3-dimensional protein folds, FASEB J. 10: 126-136.
6. Rost, B., A. Valencia. 1996. Pitfalls of protein sequence analysis. Curr: Opin. Biotech. 7: 457-461.
7. Bork, P., T. Gibson. 1996. Applying motif and profile searches. Meth. Enzym. 266: 162-184.
8. Firestine, S.M., A.E. Nixon, S.J. Benkovic. 1996. Threading your way to protein function. Chem. and Biol. 3: 779-783.
9. Casari, G., C. Sander, A. Valencia. 1995. A method to predict functional residues in proteins. Nature Struct. Biol. 2: 171-178.
10. Lichtarge, O., H.R. Bourne, F.E. Cohen. 1996. An evolutionary trace method defines binding surfaces common to protein families. J. Molec. Biol. 257: 342-358.
11. Brannigan, J.A., G. Dodson, H.J. Duggleby, P.C. Moody, J.L. Smith, D.R. Tomchick, A.G. Murzin. 1995. A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature 378: 416-419.
12. Fauman, E.B., M.A. Saper. 1996. Structure and function of the protein tyrosine phosphatases. Trends Biochem. Sci. 21: 413-417.
13. Allured, V.S., R.J. Collier, S.F. Carroll, D.B. McKay. 1986. Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Å resolution. Proc. Natl. Acad. Sci. USA 83: 1320-1324.
14. Sixma, T.K., S.E. Pronk, K.H. Kalk, E.S. Wartna, B.A.M. Van Zanten, B. Witholt, W.G.J. Hol. 1991. Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli. Nature 351: 371-377.
15. Choe, S., M.J. Bennett, G. Fujii, P.M. Curmi, K.A. Kantardjieff, R.J. Collier, D. Eisenberg. 1992. The crystal structure of diphtheria toxin. Nature 357: 216-222.
16. Weiss, M.S., S.R. Blanke, R.J. Collier, D. Eisenberg. 1995. Structure of the isolated catalytic domain of diphtheria toxin. Biochem. 34: 773-781.
17. Stein, P.E., A. Boodhoo, G.D. Armstrong, S.A. Cockle, M.H. Klein, R.J. Read. 1994. The crystal structure of pertussis toxin. Structure 2: 45-57.
18. Li, M., F. Dyda, I. Benhar, I. Pastan, D.R. Davies. 1996. 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.
19. Bell, C.E., D. Eisenberg. 1996. Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide. Biochem. 35: 1137-1149.
20. Ruf, A., J. Mennissier de Murcia, G. de Murcia, G.E. Schulz. 1996. Structure of the catalytic fragment of poly(ADP-ribose) polymerase from chicken. Proc. Natl. Acad. Sci. USA 93: 7481-7485.
21. Takada, T., K. Iida, J. Moss. 1995. Conservation of a common motif in enzymes catalyzing ADP-ribose transfer. Identification of domains in mammalian transferases. J. Biol. Chem. 270: 541-544.
22. Koch-Nolte, F., D. Petersen, S. Balasubramanian, F. Haag, D. Kahlke, T. Willer, R. Kastelein, J.F. Bazan, H.G. Thiele. 1996. Mouse T cell membrane proteins Rt6-1 and Rt6 2 are arginine/protein mono(ADPribosyl)transferases and share secondary structure motifs with ADP-ribosylating bacterial toxins. J. Biol. Chem. 271: 7686-7693.
23. Domenighini, M., R. Rappouli. 1996. Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages. Molec. Microbiol. 21: 667-674.
24. Murzin, A.G., S.E. Brenner, T. Hubbard, C. Chothia. 1995. SCOP - A Structural Classification Of Proteins database for the investigation of sequences and structures. J. Molec. Biol. 247: 536-540.
25. Holm, L., C. Sander. 1995. Dali - A network tool for protein structure comparison. Trends Biochem. Sci. 20: 478-480.
26. Rost, B., C. Sander. 1996. Bridging the protein sequence-structure gap by structure predictions. Ann. Rev. Biophys. Biomolec. Struct. 25: 113-136.
27. Sayle, R.A., E.J. Milner-White. 1995. Rasmol - Biomolecular graphics for all. Trends Biochem. Sci. 20: 374-376.
28. Reich, K.A., G.K. Schoolnik. 1996. Halovibrin, secreted from the light organ symbiont Vibrio fischeri, is a member of a new class of ADP-ribosyltransferases. J. Bacteriol. 178: 209-215.
29. Li, M., F. Dyda, I. Benhar, I. Pastan, D.R. Davies. 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.
30. Sali, A. 1995. Modeling mutations and homologous proteins. Curr. Opin. Biotech. 6: 437-451.
31. Levitt, M. 1992. Accurate modeling of protein conformation by automatic segment matching. J. Molec. Biol. 226: 507-533.
32. Chung, S.Y., S. Subbiah. 1996. A structural explanation for the twilight zone of protein sequence homology. Structure 4: 1123-1127.
33. Domenighini, M., C. Montecucco, W.C. Ripka, R. Rappuoli. 1991. Computer modeling of the NAD binding site of ADP-ribosylating toxins - active site structure and mechanism of NAD binding. Molec. Microbiol. 5: 23.
34. Marsischky, G.T., B.A. Wilson, R.J. Collier. 1995. Role of glutamic acid 988 of human poly-ADP-ribose polymerase in polymer formation. Evidence for active site similarities to the ADP-ribosylating toxins. J. Biol. Chem. 270: 3247-3254.
35. Grimaldi, J.C., S. Balasubramanian, N.H. Kabra, A. Shanafelt, J.F. Bazan, G. Zurawski, M.C. Howard. 1995. CD38-mediated ribosylation of proteins. J. Immunol. 155: 811-817.
36. Prasad, G.S., D.E. McRee, E.A. Stura, D.G. Levitt, H.C. Lee, C.D. Stout. 1996. Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectoenzyme CD38. Nature Struct. Biol. 3: 957-964.
37. Honig, B., A. Nicholls. 1995. Classical electrostatics in biology and chemistry. Science 268: 1144-1149.
38. Shao Z., F.H. Arnold. 1996. Engineering new functions and altering existing functions. Curr. Opin. Struct. Biol. 6: 513-518.