Solution structure and topology of the N-terminal membrane anchor domain of a microsomal cytochrome P450: Prostaglandin I2 synthase

Biochemical Journal

Volumn 368, Issue 3, 2002, Pages 721-728

  Ruan, Ke He ^a   So, Shui Ping ^a   Zheng, Weida ^a   Wu, Jiaxin ^a   Li, Dawei ^a   Kung, Jennifer ^a  

^a UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

Author keywords

Cytochrome P450; Membrane topology; NMR; Synthetic peptide

Indexed keywords

BIOCHEMISTRY; ENZYME KINETICS; HYDROPHOBICITY; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHOLIPIDS; SIMULATED ANNEALING;

CYTOCHROMES;

CELL MEMBRANES;

CYTOCHROME P450; DODECYLPHOSPHORYLCHOLINE; HYDROCARBON; PHOSPHOLIPID; PROSTACYCLIN SYNTHASE; TRIFLUOROETHANOL;

ARTICLE; CALCULATION; CIRCULAR DICHROISM; CONTROLLED STUDY; CYTOPLASM; ENDOPLASMIC RETICULUM; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; HUMAN CELL; HYDROPHOBICITY; MICROSOME; MOLECULAR INTERACTION; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SIMULATION;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; CYTOCHROME P-450 ENZYME SYSTEM; HUMANS; INTRAMOLECULAR OXIDOREDUCTASES; MAGNETIC RESONANCE SPECTROSCOPY; MICROSOMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXYGEN; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 0037115766     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021001     Document Type: Article

References (48)

1. Wu, K. K. and Thiagarajan, P. (1996) Role of endothelium in thrombosis and hemostasis. Annu. Rev. Med. 47, 315-331
2. DeWitt, D. L. and Smith, W. L. (1983) Purification of prostacyclin synthase from bovine aorta by immunoaffinity chromatography. Evidence that the enzyme is a hemoprotein. J. Biol. Chem. 258, 3285-3293
3. Ullrich, V., Castle, L. and Weber, P. (1981) Spectral evidence for the cytochrome p450 nature of prostacyclin synthetase. Biochem. Pharmacol. 30, 2033-2036
4. Ullrich, V. and Graf, H. (1984) Prostacyclin and thromboxane synthase as P-450 enzymes. Trends Pharmacol. Sci. 5, 352-355
5. Hara, S., Miyata, A., Yokoyama, C., Inoue, H., Brugger, R., Lottspeich, F., Ullrich, V. and Tanabe, T. (1994) Isolation and molecular cloning of prostacyclin synthase from bovine endothelial cells. J. Biol. Chem. 269, 19897-19903
6. Poulos, T. L., Finzel, B. C. and Howard, A. J. (1987) High-resolution crystal structure of cytochrome P450cam. J. Mol. Biol. 195, 697-700
7. Ravichandran, K. G., Boddupalli, S. S., Hasermann, C. A., Peterson, J. A. and Deisenhofter, J. (1993) Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450s. Science 261, 731-736
8. Hasemann, C. A., Ravichandran, K. G., Petersonn, J. A. and Deisenhofer, J. (1994) Crystal structure and refinement of cytochrome P450terp at 2.3 Å resolution. J. Mol. Biol. 236, 1169-1185
9. Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F. and McRee, D. E. (2000) Mammalian microsomal cytochrome P450 monooxygenase: Structural adaptations for membrane binding and functional diversity. Mol. Cell 5, 121-131
10. Johnson, E. F., Kronbach, T. and Hsu, M.-H. (1992) Analysis of the catalytic specificity of cytochrome P450 enzymes through site-directed mutagenesis. FASEB J. 6, 700-705
11. Zvelebil, M. J., Wolf, C. R. and Sternberg, M. J. E. (1991) A predicted three-dimensional structure of human cytochrome P450. Protein Eng. 4, 271-282
12. Tarr, G. E., Black, S. D., Fujita, V. S. and Coon, M. J. (1983) Complete amino acid sequence and predicted membrane topology of phenobarbital-induced rabbit liver microsomal cytochrome P-450 (isozyme 2). Proc. Natl. Acad. Sci. U.S.A. 80, 6552-6556
13. Ruan, K.-H., Milfeld, K., Kulmacz, R. J. and Wu, K. K. (1994) Comparison of the construction of a 3-D model for human thromboxane synthase using P450 cam and BM-3 as templates: Implications for the substrate binding pocket. Protein Eng. 7, 1345-1351
14. Nelson, D. R. and Strobel, H. W. (1988) On the membrane topology of vertebrate cytochrome P450 proteins. J. Biol. Chem. 263, 6038-6050
15. Brown, C. A. and Black, S. D. (1989) Membrane topology of mammalian cytochromes P-450 from liver endoplasmic reticulum. Determination by trypsinolysis of phenobarbital-treated microsomes. J. Biol. Chem. 264, 4442-4449
16. Vergeres, G., Winterhalter, K. H. and Richter, C. (1991) Localization of the N-terminal methionine of rat liver cytochrome P-450 in the lumen of the endoplasmic reticulum. Biochim. Biophys. Acta 1063, 235-241
17. 2-terminal substitutions of basic amino acids induce translocation across the microsomal membrane and glycosylation of rabbit cytochrome P45011C2. J. Cell Biol. 108, 1237-1243
18. Ruan, K.-H., Wang, L.-H., Wu, K.K. and Kulmacz, R. J. (1993) Amino-terminal topology of thromboxane synthase in the endoplasmic reticulum. J. Biol. Chem. 268, 19483-19490
19. Black, S. D. (1992) Membrane topology of the mammalian P450 cytochromes FASEB J. 6, 680-685
20. Edwards, R. J., Murray, B. P., Singleton, A. M. and Boobis, A. R. (1991) Orientation of cytochromes P450 in the endoplasmic reticulum. Biochemistry 30, 71-76
21. 2 synthase. J. Biol. Chem. 269, 20938-20942
22. 2 synthase and cytochrome P450 2C1. Arch. Biochem. Biophys. 352, 78-84
23. Ruan, K.-H., Stiles, B. G. and Atassi, M. Z. (1991) Full profile of the short neurotoxin-binding regions on the extracellular part of the α-chain of human acetylcholine receptor. Biochem. J. 274, 849-854
24. Moore, W. T. and Caprioli, R. M. (1991) Monitoring peptide synthesis stepwise by mass spectrometry. In Techniques in Protein Chemistry II (Villafranca, J. J., ed.), pp. 511-528, Academic Press, New York
25. Chen, Y. H., Yang, T. J. and Chau, K. H. (1974) Determination of the helix and β form of protein in aqueous solution by circular dichroism. Biochemistry 13, 3350-3359
26. Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids, John Wiley & Sons, New York
27. 2 synthase amino-terminal domain. Biochemistry 37, 822-830
28. Wüthrich, K., Billeter, M. and Braun, W. (1983) Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. J. Mol. Biol. 169, 949-961
29. 1H NMR study. Biochemistry 34, 11617-11624
30. 2 receptor. Biochemistry 40, 275-280
31. Braunschweiler, L. and Ernst, R. R. (1983) Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy. J. Magn. Reson. 53, 521-528
32. Bax, A. and Drobny, G. (1985) Optimization of two-dimensional homonuclear relayed coherence transfer NMR spectroscopy. J. Magn. Reson. 61, 306-320
33. 1H NMR spectra of proteins via double quantum filtering. Biochem. Biophys. Res. Commun. 117, 479-485
34. Jeener, J., Meier, B. H., Bachmann, P. and Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553
35. Wishart, D. S., Sykes, B. D. and Richards, F. M. (1992) The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651
36. Bystrov, V. F. (1976) Spin-spin coupling and the conformational states of peptide systems. Prog. Nucl. Magn. Reson. Spectrosc. 10, 41-82
37. Pardi, A., Billeter, M., Braun, W. and Wüthrich, K. (1984) Calibration of the angular dependence of the amide proton-Cα proton coupling constants, 3JHNα, in a globular protein. Use of 3JHNα for identification of helical secondary structure. J. Mol. Biol. 180, 741-751
38. 10-helix. J. Am. Chem. Soc. 118, 2744-2745
39. Bretscher, M. S. and Munro, S. (1993) Cholesterol and the Golgi apparatus. Science 261, 1280-1281
40. Shyue, S.-K., Ruan, K.-H., Wang, L.-H. and Wu, K. K. (1997) Prostacyclin synthase active sites. Identification by molecular modeling-guided site-directed mutagenesis. J. Biol. Chem. 272, 3657-3662
41. Ruan, K.-H., Spurlino, J., Quiocho, F. A. and Atassi, M. Z. (1990) Acetylcholine receptor-α-bungarotoxin interactions: Determination of the region to region contacts by peptide-peptide interactions and molecular modeling of the receptor cavity. Proc. Natl. Acad. Sci. U.S.A. 87, 6156-6160
42. Takemoto, D. J., Morrison, D., Davis, L. C. and Takemoto, L. J. (1986) C-terminal peptides of rhodopsin. Determination of the optimum sequence for recognition ot retinal transducin. Biochem. J. 235, 309-312
43. Konig, B., Arendt, A., McDowell, J. H., Kahlert, M., Hargrave, P. A. and Hofmann, K. P. (1989) Three cytoplasmic loops of rhodopsin interact with transducin. Proc. Natl. Acad. Sci. U.S.A. 86, 6878-6882
44. Yeagle, P. L., Alderfer, J. L. and Albert, A. D. (1995) Structure of the carboxy-terminal domain of bovine rhodopsin. Nat. Struct. Biol. 2, 832-834
45. Deng, H., Huang, A., So, S.-P., Lin, Y.-Z. and Ruan, K.-H. (2002) Substrate access channel topology in membrane-bound prostacyclin synthase. Biochem. J. 326, 545-551
46. 2 synthase. Nature (London) 367, 243-249
47. 2 biosynthesis. J. Biol. Chem. 264, 141-150
48. 2 synthase active site residues by molecular modeling-guided site-directed mutagenesis. J. Biol. Chem. 271, 19970-19975