The crystal structure of nitrophorin 4 at 1.5 Å resolution: Transport of nitric oxide by a lipocalin-based heme protein

Structure

Volumn 6, Issue 10, 1998, Pages 1315-1327

  Andersen, John F ^a   Weichsel, Andrzej ^a   Balfour, Celia A ^a   Champagne, Donald E ^b   Montfort, William R ^a  

^a University of Arizona   (United States)

^b UNIVERSITY OF GEORGIA   (United States)

Author keywords

Bilin binding protein; Histamine; Lipocalin; Rhodnius prolixus; Vasodilator; X ray crystallography

Indexed keywords

ANIMALIA; ESCHERICHIA COLI; HEXAPODA; INSECTA; RHODNIUS; RHODNIUS PROLIXUS; TRYPANOSOMA; TRYPANOSOMA CRUZI;

EID: 0032532483     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00131-2     Document Type: Article

References (39)

1. Law, J., Ribeiro, J.M.C. & Wells, M. (1992). Biochemical insights derived from diversity in insects. Annu. Rev. Biochem. 61, 87-111.
2. Champagne, D.E., Nussenzvieg, R.H. & Ribeiro, J.M.C. (1995). Purification, partial characterization and cloning of nitric oxide-carrying heme proteins (nitrophorins) from salivary glands of the blood-sucking insect Rhodnius prolixus. J. Biol. Chem. 270, 8691-8695.
3. Kirchhoff, L.V. (1993). American trypanosomiasis (Chagas' Disease) - A tropical disease now in the United States. N. Engl. J. Med. 329, 639-644.
4. Ribeiro, J.M.C., Hazzard, J.M.H., Nussenzveig, R.H., Champagne, D.E. & Walker, F.A. (1993). Reversible binding of nitric oxide by a salivary heme protein from a bloodsucking insect. Science 260, 539-541.
5. Ribeiro, J.M.C. & Walker, F.A. (1994). High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus. J. Exp. Med. 180, 2251 -2257.
6. Weichsel, A., Andersen, J.F., Champagne, D.E., Walker, F.A. & Montfort, W.R. (1998). Crystal structures of a nitric oxide transport protein from a blood-sucking insect. Nat. Struct. Biol. 5, 304-309.
7. Ribeiro, J.M.C. (1982). The antiserotonin and antihistamine activities of salivary secretion of Rhodnius prolixus. J. Insect. Physiol. 28, 69-75.
8. Flower, D.R. (1996). The lipocalin protein family: structure and function. Biochem. J. 318, 1-14.
9. Holden, H.M., Rypniewski, W.R., Law, J.H. & Rayment, I. (1987). The molecular structure of insecticyanin from the tobacco hornworm Manduca sexta L. at 2.6 A resolution. EMBO J. 6, 1565-1570.
10. Huber, R., et al., & Kayser, H. (1987). Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 Å resolution. J. Mol. Biol. 198, 499-513.
11. 2 subunits with astaxanthin. Eur. J. Biochem. 202, 31-40.
12. Noeske-Jungblut, C., et al., & Shleuning, W.-D. (1994). An inhibitor of collagen-induced platelet aggregation from the saliva of Triatoma pallidipennis. J. Biol. Chem. 269, 5050-5053.
13. Noeske-Jungblut, C., Haendler, B., Donner, P., Alagon, A., Possani, L., Schleuning, W.-D. (1995). Triabin, a highly potent exosite inhibitor of thrombin. J. Biol. Chem. 270, 28629-28634.
14. Andersen, J.F., et al., & Montfort, W.R. (1997). Nitric oxide binding and crystallization of recombinant nitrophorin I, a nitric oxide transport protein from the blood-sucking bug Rhodnius prolixus. Biochemistry 36, 4423-4428.
15. Ribeiro, J.M.C. (1996). Salivary thiol oxidase activity of Rhodnius prolixus. Insect Biochem. Mol. Biol. 26, 899-905.
16. Ribeiro, J.M.C., Schneider, M. & Guimaraes, J.A. (1995). Purification and characterization of prolixin S (nitrophorin 2), the salivary anticoagulant of the blood-sucking bug Rhodnius prolixus. Biochem. J. 308, 243-249.
17. Sun, J., et al., & Chinzei, Y. (1996). Purification, characterization and cDNA cloning of a novel anticoagulant of the intrinsic pathway (prolixin-S) from salivary glands of the blood sucking bug, Rhodnius prolixus. Thromb. Haemost. 75, 573-577.
18. Olson, J.S. & Phillips, G.N., Jr. (1996). Kinetic pathways and barriers for ligand binding to myoglobin. J. Biol. Chem. 271, 17596.
19. Newcomer, M.E., et al., & Peterson, P.A. (1984). The three-dimensional structure of retinol-binding protein. EMBO J. 3, 1451-1454.
20. Brownlow, S., et al., & Sawyer, L. (1997). Bovine beta-lactoglobulin at 1.8 Å resolution - still an enigmatic lipocalin. Structure 5, 481-495.
21. Newcomer, M.E. (1993). Structure of the epididymal retinoic acid binding protein at 2.1 Å resolution. Structure 1, 7-18.
22. Flower, D.R., North, A.C.T. & Attwood, T.K. (1993). Structure and sequence relationships in the lipocalins and related proteins. Protein Sci. 2, 753-761.
23. Haendler, B., Becker, A., Noeske-Jungblut, C., Kratzschmar, J., Donner, P. & Schleuning, W.-D. (1995). Expression of active recombinant pallidipin, a novel platelet aggregation inhibitor, in the periplasm of Escherichia coli. Biochem. J. 307, 465-470.
24. Fuentes-Prior, P., Noeske-Jungblut, C., Donner, P., Schleuning, W.-D., Huber, R. & Bode, W. (1997). Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug. Proc. Natl Acad. Sci. USA 94, 11845-11850.
25. Hawkins, B.K., Wilks, A., Powers, L.S., Ortiz de Montellano, P.R. & Dawson, J.H. (1996). Ligation of the iron in the heme-heme oxygenase complex: X-ray adsorption, electronic absorption and magnetic circular dichroism studies. Biochem. Biophys. Acta 1295, 165-173.
26. Yoshida, T. & Kikuchi, G. (1978). Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oygenase system. J. Biol. Chem. 253, 4230-4236.
27. O'Carra, P. (1975). Heme-cleavage: Biological systems and chemical analogs. In Porphyrins and Metalloporphyrins, (Smith, K.M., ed) pp. 124-153, Elsevier Science, Amsterdam.
28. Kayser, H. (1985). Pigments. In Comprehensive Insect Physiology, Biochemistry, and Pharmacology, Vol. 9. (Kerkut, G.A. & Gilbert, L.I., eds) pp. 367-415, Pergamon Press, Oxford.
29. Messerschmidt, A. & Pflugrath, J.W. (1987). Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography. J. Appl. Cryst. 20, 306-315.
30. Kabsch, W. (1988). Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Cryst. 21, 916-934.
31. Collaboratative Computational Project, Number 4. (1994). CCP4. The CCP4 Suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
32. Brünger, A.T. (1992). X-PLOR Version 3.1. A System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT.
33. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
34. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
35. Kleywegt, G.J. & Jones, TA (1995). Where freedom is given, liberties are taken. Structure 3, 535-540.
36. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
37. Bacon, D.J. & Anderson, W.F. (1988). A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graph. 6, 219-220.
38. Merritt, E.A. & Murphy, M.E.P. (1994). Raster3D Version 2.0 - A program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
39. Brünger, AT. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.