Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs

Nature Structural Biology

Volumn 5, Issue 12, 1998, Pages 1091-1097

  Bhatnagar, Rajiv S ^a   Fütterer, Klaus ^a   Farazi, Thalia A ^a   Korolev, Sergey ^a   Murray, Clare L ^a   Jackson Machelski, Emily ^a   Gokel, George W ^a   Gordon, Jeffrey I ^a   Waksman, Gabriel ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; CARBOXYLIC ACID DERIVATIVE; PEPTIDE DERIVATIVE; PROTEIN N MYRISTOYLTRANSFERASE;

DRUG TARGETING; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; REVIEW; SACCHAROMYCES CEREVISIAE;

ACYL COENZYME A; ACYLTRANSFERASES; AMINO ACID SEQUENCE; BINDING SITES; CANDIDA ALBICANS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; FUNGAL PROTEINS; GLYCINE; IMIDAZOLES; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; MYRISTIC ACID; OLIGOPEPTIDES; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES POMBE PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0031788774     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/4202     Document Type: Review

References (35)

1. Towler, D.A. et al. Purification and characterization of myristoylCoA:protein N-myristoyltransferase. Proc. Natl. Acad Sci. USA 84, 2708-2712 (1987).
2. Boutin, J. Myristoylation. Cell. Signal. 9, 15-35 (1997).
3. Bhatnagar, R. S. & Gordon, J. I. Understanding covalent modifications of proteins by lipids: where cell biology and biophysics mingle. Trends Cell Biol. 7, 14-18 (1997).
4. Bryant, M. L. et al. Incorporation of 12-methoxydodecanoate into the human immunodeficiency virus I gag polyprotein precursor inhibits its proteolytic processing and viral production in a chronically infected human lymphoid cell line. Proc. Natl. Acad. Sci. USA 88, 2055-2059 (1991).
5. Duronio, R. J., Towler, D. A., Heuckeroth, R. O. & Gordon, J. I. Disruption of the yeast N-myristoyl transferase gene causes recessive lethality. Science 243, 796-800 (1989).
6. Weinberg, R. A. et al. Genetic studies reveal that myristoylCoA:protein N-myristoyltransferase is an essential enzyme in Candida albicans. Mol. Microbiol. 16, 241-250 (1995).
7. Lodge, J. K., Jackson-Machelski, E., Toffaletti, D. L., Perfect, J. R. & Gordon, J. I. Targeted gene replacement demonstrates that myristoylCoA:protein N-myristoyltransferase is essential for viability of Cryptococcus neoformans. Proc. Natl. Acad. Sci. USA 91, 12008-12012 (1994).
8. Sikorski, J. A. et al. Selective peptidic and peptidomimetic inhibitors of Candida albicans myristoylCoA:protein N-myristoyltransferase: A new approach to antifungal therapy. Biopolymers 43, 43-71 (1997).
9. White, T. C., Marr, K. A. & Bowden, P. A. Clinical, cellular, and molecular factors that contribute to antifungal drug resistance. Clin. Microbiol. Rev. 11, 382-402 (1998).
10. Rudnick, D. A. et al. Kinetic and structural evidence for a sequential ordered Bi Bimechanism of catalysis by Saccharomyces cerevisiae myristoylCoA:protein N myristoyltransferase. J. Biol. Chem. 266, 9732-9739 (1991).
11. Bhatnagar, R. S. et al. Titration calorimetric analysis of acylCoA recognition by myristoylCoA:protein N-myristoyltransferase. Biochemistry 36, 6700-6708 (1997).
12. Rocque, W. J., McWherter, C. A., Wood, D. C. & Gordon, J. I. A comparative analysis of the kinetic mechanism and peptide substrate specificity of human and Saccharomyces cerevisiae myristoylCoA:protein N-myristoyltransferase. J. Biol. Chem. 268, 9964-9971 (1993).
13. Weston, S. A. et al. Crystal structure of the anti-fungal targed N-myristoyltransferase. Nature Struct. Biol. 5, 213-221 (1998).
14. Paige, L. A., Zheng, G-Q., DeFrees, S. A., Cassady, J. M. & Geahlen, R. L. S-(2-oxopentadecyl)-CoA, a nonhydrolyzable analog of myristoylCoA, is a potent inhibitor of myristoylCoA:protein N-myristoyltransferase. J. Med. Chem., 32, 1665-1667 (1989).
15. Devadas, B. et al. Design and synthesis of potent and selective dipeptide inhibitors of Candida albicans myristoylCoA:protein N-myristoyltransferase. J. Med. Chem., 38, 1837-1840 (1995).
16. Rudnick, D. A. et al. Analogs of palmitoylCoA that are substrates for myristoylCoA:protein N-myristoyltransferase. Proc. Natl. Acad. Sci. USA 89, 10507-10511 (1992).
17. Towler, D. A., Gordon, J. I., Adams, S. P. & Glaser, L. The biology and enzymology of eukaryotic protein acylation. Annu. Rev. Biochem. 57, 69-99 (1988).
18. Bairoch, A., Bucher, P. & Hofmann, K. The PROSITE database, its status in 1997. Nucleic Acids Res. 25, 217-221 (1997).
19. Zhang, L., Jackson-Machelski, E. & Gordon, J. I. Genetic and biochemical studies of S. cerevisiae myristoylCoA:protein N-myristoyltransferase mutants. J. Biol. Chem. 271, 33131-33140 (1996).
20. Peseckis, S.M. & Resh, M.D. Fatty acyl transfer by N-myristyl transferase is dependent upon conserved cysteine and histidine residues. J. Biol. Chem. 269, 30888-30892 (1994).
21. Rudnick, D. A., Johnson, R. L. & Gordon, J. I. Studies of the catalytic activities and substrate specificities of Saccharomyces cerevisiae myristoylCoA:protein N-myristoyltransferase deletion mutants and human/yeast Nmt chimeras in Eschericia coli and S. cerevisiae . J. Biol. Chem. 267, 23852-23861 (1992).
22. Zheng, W., Johnston, S. A. & Joshua-Tor, L. The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase. Cell 93, 103-109 (1998).
23. Hendrickson, W. A., Horton, J. R. & LeMaster, D. Selenomethionine proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9, 1665-1672 (1990).
24. Otwinowski, Z. in Proceedings of the CCP4 study weekend: data collection and processing. (eds Sawyers, L. Isaacs, N. & Bailey, S.) 56-62 (SERC Daresbury Laboratory, Warrington, UK; 1993).
25. Terwilliger, T. C., Kim, S.-H. & Eisenberg, D. Generalized method of determining heavy-atom positions using the difference Patterson function. Acra Crystallogr. A 43, 1-5 (1987).
26. De La Fortelle, E. & Bricogne, G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Meth. Enz. 276, 472-493 (1997).
27. Abrahams, J. P. & Leslie, A. G. W. Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acts Crystallogr. D52, 32-42 (1996).
28. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119 (1991).
29. Terwilliger, T. C. & Eisenberg, O. Unbiased Three-Dimensional Refinement of Heavy-Atom Parameters by Correlation of Origin-Removed Patterson Functions. Acta Crystallogr. A39, 813-817 (1983).
30. Hall, T. M. T., Porter, J. A., Beachy, P. A. & Leahy, D. J. A potential catalytic site revealed by the 1.7Å crystal structure of the amino-terminal signalling domain of Sonic hedgehog. Nature 378, 212-216 (1995).
31. Brünger, A. T. et al. Crystallography and NMR system: a new software system for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
32. Brünger, A. T. The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474 (1992).
33. Carson, M. Ribbons. Meth. Enz. 277, 493-505 (1997).
34. Nicholls, A. & Honig, B. A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzman equation. J. Comput. Chem. 12, 435-445 (1991).
35. Engh, R. A. & Huber, R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A47, 392-400 (1991).