A molecular switch and proton wire synchronize the active sites in thiamine enzymes

Science

Volumn 306, Issue 5697, 2004, Pages 872-876

  Frank, René A W ^a   Titman, Christopher M ^a   Pratap, J Venkatesh ^a   Luisi, Ben F ^a   Perham, Richard N ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENZYMES; POLYPEPTIDES; SYNCHRONIZATION; WIRE;

CHEMICAL EVENTS; MOLECULAR SWITCHES; SHUTTLING; THIAMINE DIPHOSPHATE (THDP);

PROTONS;

COCARBOXYLASE; PYRUVATE DEHYDROGENASE; THIAMINE DERIVATIVE;

BIOLOGY;

ARTICLE; CATALYSIS; CONFORMATION; ENZYME KINETICS; GEOBACILLUS STEAROTHERMOPHILUS; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SUBSTITUTION; BACILLUS STEAROTHERMOPHILUS; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; KINETICS; MODELS, MOLECULAR; MUTATION; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PROTONS; PYRUVATE DEHYDROGENASE (LIPOAMIDE); PYRUVATE DEHYDROGENASE COMPLEX; PYRUVIC ACID; THIAMINE PYROPHOSPHATE;

GEOBACILLUS STEAROTHERMOPHILUS;

EID: 7444244483     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1101030     Document Type: Article

References (35)

1. N. K. Nagradova, FEBS Lett. 487, 327 (2001).
2. A. Schellenberger, Biochim. Biophys. Acta 1385, 177 (1998).
3. F. Horn, H. Bisswanger, J. Biol. Chem. 258, 6912 (1983).
4. R. Breslow, J. Am. Chem. Soc. 79, 1762 (1957).
5. A. Schellenberger, G. Hübner, H. Neef, Methods Enzymol. 279, 131 (1997).
6. F. Jordan et al., J. Am. Chem. Soc. 125, 12732 (2003).
7. Y. Lindqvist, G. Schneider, U. Ermler, M. Sundstrom, EMBO J. 11, 2373 (1992).
8. D. Kern et al., Science 275, 67 (1997).
9. M. E. Caines, J. M. Elkins, K. S. Hewitson, C. J. Schofield, J. Biol. Chem. 279, 5685 (2004).
10. M. Fries, H. I. Jung, R. N. Perham, Biochemistry 42, 6996 (2003).
11. N. Nemeria et al., Biochemistry 41, 15459 (2002).
12. R. N. Perham, Annu. Rev. Biochem. 69, 961 (2000).
13. I. A. Lessard, C. Fuller, R. N. Perham, Biochemistry 35, 16863 (1996).
14. H. J. Chauhan, G. J. Domingo, H. I. Jung, R. N. Perham, Eur. J. Biochem. 267, 7158 (2000).
15. D. D. Jones, K. M. Stott, P. A. Reche, R. N. Perham, J. Mol. Biol. 305, 49 (2001).
16. R. A. W. Frank, J. V. Pratap, X. Y. Pei, R. N. Perham, B. Luisi, in preparation.
17. T. Nakai et al., J. Mol. Biol. 337, 1011 (2004).
18. A. Ævarsson, K. Seger, S. Turley, J. R. Sokatch, W. G. Hol, Nature Struct. Biol. 6, 785 (1999).
19. A. Ævarsson et al., Structure Fold. Des. 8, 277 (2000).
20. E. M. Ciszak, L. G. Korotchkina, P. M. Dominiak, S. Sidhu, M. S. Patel, J. Biol. Chem. 278, 21240 (2003).
21. P. Arjunan et al., Biochemistry 41, 5213 (2002).
22. M. Nikkola, Y. Lindqvist, G. Schneider, J. Mol. Biol. 238, 387 (1994).
23. Supporting data are available on Science Online.
24. M. Sundstrom, Y. Lindqvist, G. Schneider, FEBS Lett. 313, 229 (1992).
25. X. Huang, H. M. Holden, F. M. Raushel, Annu. Rev. Biochem. 70, 149 (2001).
26. D. Hawksley, D. A. Griffin, F. J. Leeper, J. Chem. Soc. [Perkin 1] 2001, 144 (2001).
27. W. Lattimer, W. Rodebush, J. Am. Chem. Soc. 42, 1419 (1920).
28. H. Bisswanger, U. Henning, Eur. J. Biochem. 24, 376 (1971).
29. G. Lu, D. Dobritzsch, S. Baumann, G. Schneider, S. Konig, Eur. J. Biochem. 267, 861 (2000).
30. A. Levitzki, D. E. Koshland Jr., Curr. Top. Cell. Regul. 10, 1 (1976).
31. A. Szoke, W. G. Scott, J. Hajdu, FEBS Lett. 553, 18 (2003).
32. P. H. Sugden, P. J. Randle, Biochem. J. 173, 659 (1978).
33. E. A. Sergienko, F. Jordan, Biochemistry 41, 3952 (2002).
34. F. Jordan, Nat. Prod. Rep. 20, 184 (2003).
35. We are grateful to D. Hawksley and F. Leeper (Chemical Laboratory, University of Cambridge) for the generous gift of deazathiamine diphosphate and advice. We thank L. Packman and co-workers from the PNAC, Department of Biochemistry, University of Cambridge, for the synthesis of oligonucleotides and N-terminal sequencing and H. Dixon for stimulating discussions and many helpful comments. This work was supported by grants from the Biotechnology and Biological Sciences Research Council (BBSRC) and the Wellcome Trust The coordinates and structure factors of the E1-PSBD and E1 (NQ)-PSBD have been deposited at the Protein Data Bank (accession code 1w85 and 1w88, respectively).