The structure of nitric oxide synthase oxygenase domain and inhibitor complexes

Science

Volumn 278, Issue 5337, 1997, Pages 425-431

  Crane, Brian R ^a,c   Arvai, Andrew S ^a   Gachhui, Ratan ^b   Wu, Chaoqun ^b   Ghosh, Dipak K ^b   Getzoff, Elizabeth D ^a   Stuehr, Dennis J ^b   Tainer, John A ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b LERNER RESEARCH INSTITUTE   (United States)

^c CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOGUANIDINE; ARGININE; HEME; IMIDAZOLE; NITRIC OXIDE SYNTHASE; OXYGEN; OXYGENASE;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME INHIBITOR COMPLEX; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBUNIT; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ARGININE; BINDING SITES; BIOPTERIN; CAENORHABDITIS ELEGANS PROTEINS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENZYME INDUCTION; ENZYME INHIBITORS; GUANIDINES; HEME; HOMEODOMAIN PROTEINS; HYDROGEN BONDING; IMIDAZOLES; ISOENZYMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NITRIC OXIDE SYNTHASE; OXIDATION-REDUCTION; OXYGEN; OXYGENASES; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 0030723329     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.278.5337.425     Document Type: Article

References (54)

1. S. Moncada and A. Higgs, N. Eng. J. Med. 329, 2002 (1993); C. Nathan and Q. Xie, Cell 78, 915 (1994); H. H. Schmidt and U. Walter, ibid., p. 919.
2. S. Moncada and A. Higgs, N. Eng. J. Med. 329, 2002 (1993); C. Nathan and Q. Xie, Cell 78, 915 (1994); H. H. Schmidt and U. Walter, ibid., p. 919.
3. S. Moncada and A. Higgs, N. Eng. J. Med. 329, 2002 (1993); C. Nathan and Q. Xie, Cell 78, 915 (1994); H. H. Schmidt and U. Walter, ibid., p. 919.
4. O. W. Griffith and D. J. Stuehr, Annu. Rev. Physiol. 57, 707 (1995).
5. G. J. Southan and C. Szabo, Biochem. Pharmacol. 51, 383 (1996).
6. B. Mayer and E. R. Werner, Nauyn-Schmiedebergs Arch. Phamacol. 351, 453 (1995).
7. B. S. S. Masters et al., FASEB J. 10, 552 (1996).
8. E. J. Mueller, P. J. Loida, S. G. Sligar, in Cytochrome P450: Structure, Mechanism, and Biochemistry, P. R. Ortiz de Montellano, Ed. (Plenum, New York, 1995), pp. 83-124.
9. M. Sono, M. P. Roach, E. D. Coulter, J. H. Dawson, Chem. Rev. 96, 2841 (1996).
10. M. Marletta, Cell 78, 927 (1994).
11. D. Stuehr, Annu. Rev. Pharmacol. Toxicol. 18, 707 (1997).
12. D. K. Ghosh et al., Biochemistry 36, 10609 (1997).
13. D. K. Ghosh, R. Gachhui, C. Wu, N. Sennequier, H. M. Abu-Soud, D. J. Stuehr, unpublished results.
14. I. Rodriguez-Crespo, P. Moënne-Loccoz, T. M. Loehr, P. R. Ortiz de Montellano, Biochemistry 36, 8530 (1997).
15. ox Δ114 crystal in 10 mM aminoguanidine carbonate, 40 mM Hepes, pH 7.9, and 12% PEG MW 6000 for 30 hours.
16. free determined if regions with high B values were included in the model.
17. free determined if regions with high B values were included in the model.
18. free determined if regions with high B values were included in the model.
19. free determined if regions with high B values were included in the model.
20. free determined if regions with high B values were included in the model.
21. free determined if regions with high B values were included in the model.
22. free determined if regions with high B values were included in the model.
23. free determined if regions with high B values were included in the model.
24. free determined if regions with high B values were included in the model.
25. 2 for aminoguanidine) reflects more overall order in the orthorhombic aminoguanidine complex compared with the imidazole complex.
26. ox is similar in both crystal forms.
27. ox is similar in both crystal forms.
28. L. Holm and C. Sander, J. Mol. Biol. 233, 123 (1993).
29. F. C. Bernstein et al., ibid. 112, 535 (1977).
30. M. Sono, D. J. Stuehr, M. Ikeda-Saito, J. K. Dawson, J. Biol. Chem. 270, 19943 (1996).
31. J. C. Salerno, K. McMillan, B. S. S. Masters, Biochemistry 35, 11839 (1996).
32. Q. W. Xie, M. Leung, M. Fuortes, S. Sassa, C. Nathan, Proc. Natl. Acad. Sci. U.S.A. 93, 4891 (1996).
33. J. Wang, D. J. Stuehr, D. L. Rousseau, Biochemistry 36, 4595 (1997).
34. P. F. Chen, A. L. Tsai, V. Berka, K. Wu, J. Biol. Chem. 272, 6114 (1997).
35. R. Gachhui et al., Biochemistry 36, 5097 (1997).
36. D. Mansuy and J. P. Renaud, in (6), pp. 537-574.
37. M. Sundaramoorthy, J. Terner, T. L. Poulos, Structure 3, 1367 (1995).
38. N. Sennequier and D. J. Stuehr, Biochemistry 35, 5883 (1996).
39. R. M. Chabin et al., ibid., p. 9567.
40. D. J. Wolff and A. Lubeskie, Arch. Biochem. Biophys. 316, 290 (1995).
41. J. Wang, D. Rousseau, H. M. Abu-Soud, D. J. Stuehr, Proc. Natl. Acad. Sci. U.S.A. 91, 10512 (1994).
42. H. M. Abu-Soud, R. Gachhui, F. M. Raushel, D. J. Stuehr, J. Biol. Chem. 271, 17349 (1997).
43. B. R. Crane et al., data not shown.
44. T. L. Poulos, J. Cupp-Vickery, H. Li, in (6), pp. 125-150.
45. M. Wang, D. L. Roberts, R. Paschke, T. M. Shea, B. S. S. Masters, Proc. Natl. Acad. Sci. U.S.A. 94, 8411 (1997).
46. A. D. N. Vaz, S. J. Pernecky, G. M. Raner, M. J. Coon, ibid. 93, 4644 (1996).
47. D. B. Goodin, M. G. Davidson, J. A. Roe, A. G. Mauk, M. Smith, Biochemistry 30, 4953 (1991).
48. L. Vitello, J. Erman, M. Miller, J. Wang, J. Kraut, ibid. 32, 9807 (1993).
49. T. Brittain, R. Blackmore, C. Greenwood, A. J. Thompson, Eur. J. Biochem. 209, 793 (1992).
50. U. Siddhanta et al., J. Biol. Chem. 271, 7309 (1996).
51. D. E. McRee, J. Mol. Graphics 10, 44 (1992).
52. These three NOS structures have excellent stereochemistry with 98.8% of all residues falling in the most favored or otherwise allowed regions of a Ramachandran φ/ψ plot, as defined by PROCHECK [R. A. Laskowski et al., J. Appl. Crystallogr. 26, 283 (1993)]. No residues fall in disallowed regions. Nonbonded contacts were assessed with ERRAT [C. Colovos and T. O. Yeates, Protein Sci. 2, 1511 (1993)] and found to be as likely or more likely than those of a representative group of high-resolution protein structures.
53. These three NOS structures have excellent stereochemistry with 98.8% of all residues falling in the most favored or otherwise allowed regions of a Ramachandran φ/ψ plot, as defined by PROCHECK [R. A. Laskowski et al., J. Appl. Crystallogr. 26, 283 (1993)]. No residues fall in disallowed regions. Nonbonded contacts were assessed with ERRAT [C. Colovos and T. O. Yeates, Protein Sci. 2, 1511 (1993)] and found to be as likely or more likely than those of a representative group of high-resolution protein structures.
54. We thank C. Mol, C. Putnam, A. Bilwes, and J. Noel for help with data collection, A. Bilwes and D. Goodin for helpful discussions, P. Clark, T. Macke, and J. Zhang for technical assistance, and SSRL for use of data collection facilities. Supported by NIH grants HL58883 and CA53914. D.J.S. is an Established Investigator of the American Heart Association.