A close family resemblance: The importance of structure in understanding cytochromes P450

Structure

Volumn 6, Issue 9, 1998, Pages 1079-1085

  Peterson, Julian A ^a   Graham, Sandra E ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0032530250     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00109-9     Document Type: Article

References (28)

1. Omura, T. & Sato, R. (1964). The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem. 239, 2370-2378.
2. Omura, T., Sato, R., Cooper, D.Y., Rosenthal, O. & Estabrook, R.W. (1965). Function of cytochrome P-450 of microsomes. Fed. Proc. 24, 1181-1189.
3. Nelson, D.R., et al., & Nebert, D.W. (1996). P450 superfamily: update on new sequences, gene mapping, accession numbers and nomenclature. Pharmacogenetics 6, 1-42.
4. Hasemann, C.A., Kurumbail, R.G., Boddupalli, S.S., Peterson, J.A. & Deisenhofer, J. (1995). Structure and function of cytochromes P450: a comparative analysis of three crystal structures. Structure 3, 41-62.
5. Poulos, T.L., Finzel, B.C. & Howard, A.J. (1987). High-resolution crystal structure of cytochrome P450cam. J. Mol. Biol. 195, 687-700.
6. Ravichandran, K.G., Boddupalli, S.S., Hasemann, C.A., Peterson, J.A. & Deisenhofer, J. (1993). Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's. Science 261, 731-736.
7. Hasemann, C.A., Ravichandran, K.G., Peterson, J.A. & Deisenhofer, J. (1994). Crystal structure and refinement of cytochrome P450terp at 2.3 Å resolution. J. Mol. Biol. 236, 1169-1185.
8. Cupp-Vickery, J.R. & Poulos, T.L. (1995). Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nat. Struct. Biol. 2, 144-153.
9. Park, S.Y., et al., & Shiro, Y. (1997). Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum. Nat. Struct. Biol. 4, 827-832.
10. Poulos, T.L., Finzel, B.C., Gunsalus, I.C., Wagner, G.C. & Kraut, J. (1985). The 2.6-Å crystal structure of Pseudomonas putida cytochrome P-450. J. Biol. Chem. 260, 16122-16130.
11. Ozols, J., Heinemann, F.S. & Johnson, E.F. (1985). The complete amino acid sequence of a constitutive form of liver microsomal cytochrome P-450. J. Biol. Chem. 260, 5427-5434.
12. Gotoh, O. (1992). Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J. Biol. Chem. 267, 83-90.
13. 2-terminal region and expressed in Escherichia coli. Arch. Biochem. Biophys. 318, 446-456.
14. Graham-Lorence, S.E., Amarneh, B., White, R.E., Peterson, J.A. & Simpson, E.R. (1995). A three-dimensional model of aromatase cytochrome P450. Protein Sci. 4, 1065-1080.
15. Paulsen, M.D. & Ornstein, R.L. (1995). Dramatic differences in the motions of the mouth of open and closed cytochrome P450BM-3 by molecular dynamics simulations. Proteins 21, 237-243.
16. Arnold, G.E. & Ornstein, R.L. (1997). Molecular dynamics study of time-correlated protein domain motions and molecular flexibility: cytochrome P450BM-3. Biophys. J. 73, 1147-1159.
17. Modi, S., Sutcliffe, M.J., Primrose, W.U., Lian, L.Y. & Roberts, G.C. (1996). The catalytic mechanism of cytochrome P450 BM3 involves a 6 Å movement of the bound substrate on reduction. Nat. Struct. Biol. 3, 414-417.
18. Li, H. & Poulos, T.L. (1996). Conformational dynamics in cytochrome P450-substrate interactions. Biochimie 78, 695-699.
19. αβγ binding surfaces support a model of the G protein-receptor complex. Proc. Natl Acad. Sci. USA 93, 7507-7511.
20. Lichtarge, O., Bourne, H.R. & Cohen, F.E. (1996). An evolutionary trace method defines binding surfaces common to protein families. J. Mol. Biol. 257, 342-358.
21. Needleman, S.B. & Wunsch, C.D. (1970). A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48, 443-453.
22. Benson, D.E., Suslick, K.S. & Sugar, S.G. (1997). Reduced oxy intermediate observed in D251 N cytochrome P450cam. Biochemistry 36, 5104-5107.
23. Shen, S. & Strobel, H.W. (1992). The role of cytochrome P450 lysine residues in the interaction between cytochrome P450lA1 and NADPH-cytochrome P450 reductase. Arch. Biochem. Biophys. 294, 83-90.
24. Wang, M., Roberts, D.L., Paschke, R., Shea, T.M., Masters, B.S. & Kim, J.J.P. (1997). Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. Proc. Natl Acad. Sci. USA 94, 8411-8416.
25. Wada, A. & Waterman, M.R. (1992). Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding. J. Biol. Chem. 267, 22877-22882.
26. Cawley, G.F., Batie, C.J. & Backes, W.L. (1995). Substrate-dependent competition of different P450 isozymes for limiting NADPH-cytochrome P450 reductase. Biochemistry 34, 1244-1247.
27. Connolly, M.L. (1983). Solvent-accessible surfaces of proteins and nucleic acids. Science 221, 709-713.
28. Graham-Lorence, S.E., et al., & Capdevila, J.H. (1997). An active site substitution, F87V, converts cytochrome P450 BM-3 into a regio- and stereoselective (14S, 15R)-arachidonic acid epoxygenase. J. Biol. Chem. 272, 1127-1135.