Solution structure of a chemosensory protein from the desert locust Schistocerca gregaria

Biochemistry

Volumn 45, Issue 35, 2006, Pages 10606-10613

  Tomaselli, Simona ^a   Crescenzi, Orlando ^a   Sanfelice, Domenico ^a   Eiso, A B ^b,e   Wechselberger, Rainer ^b   Angeli, Sergio ^c   Scaloni, Andrea ^d   Boelens, Rolf ^b   Tancredi, Teodorico ^d   Pelosi, Paolo ^c   Picone, Delia ^a  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b UTRECHT UNIVERSITY   (Netherlands)

^c UNIVERSITY OF PISA   (Italy)

^d CNR   (Italy)

^e LEIDEN UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOSENSORS; CONFORMATIONS; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; VOLATILE ORGANIC COMPOUNDS;

CHEMOSENSORY PROTEINS (CSP); DESERT LOCUST SCHISTOCERCA GREGARIA; HYDROPHOBIC CAVITIES;

PROTEINS;

CHEMOSENSORY PROTEIN; INSECT PROTEIN; OLEAMIDE; PROTEIN CSPSG4; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BETA CHAIN; CONFORMATIONAL TRANSITION; HYDROPHOBICITY; LIGAND BINDING; LOCUST; MOTH; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; SPECIES COMPARISON; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; GRASSHOPPERS; INSECT PROTEINS; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

HEXAPODA; INSECTA; LEPIDOPTERA; MAMESTRA BRASSICAE; SCHISTOCERCA GREGARIA;

EID: 33748264951     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060998w     Document Type: Article

References (55)

1. Clyne, P. J., Warr, C. G., Freeman, M. R., Lessing, D., Kim, J., and Carlson, J. R. (1999) A novel family of divergent seven-transmembrane proteins: candidate odorant receptors in Drosophila, Neuron 22, 327-338.
2. Vosshall, L. B., Amrein, H., Morozov, P. S., Rzhetsky, A., and Axel, R. (1999) A spatial map of olfactory receptor expression in the Drosophila antenna, Cell 96, 725-736.
3. Pelosi, P., and Maida, R. (1995) Odorant-binding proteins in insects, Comp. Biochem. Physiol. 111B, 503-514.
4. Pelosi, P. (1998) Odorant-binding proteins: structural aspect, Ann. N.Y. Acad. Sci. 855, 281-293.
5. Steinbrecht, R. (1998) Odorant-binding proteins: expression and function, Ann. N.Y. Acad. Sci. 855, 323-332.
6. Picimbon, J. F. (2003) Biochemistry and evolution of OBP and CSP proteins, in Insect Pheromone Biochemistry and Molecular Biology (Blomquist, G. J., and Vogt, R. G., Eds.) pp 539-566, Elsevier Academic Press, London.
7. Vogt, R. G. (2003) Biochemical diversity of odor detection: OBPs, ODEs and SNMPs, in Insect Pheromone Biochemistry and Molecular Biology (Blomquist, G. J., and Vogt, R. G., Eds.) pp 391-446, Elsevier Academic Press, London.
8. Vogt, R. G. (2005) Molecular basis of pheromone detection in insects, in Comprehensive Insect Physiology, Biochemistry, Pharmacology and Molecular Biology. Volume 3. Endocrinology (Gilbert, L. I., Iatro, K., and Gill, S., Eds.) pp 753-804, Elsevier, London.
9. Wanner, K. W., Willis, L. G., Theilmann, D. A., Isman, M. B., Feng, Q., and Plettner, E. (2004) Analysis of the insect OS-D-like gene family, J. Chem. Ecol. 30, 889-911.
10. Pelosi, P., Zhou, J. J., Ban, L. P., and Calvello, M. (2006) Soluble proteins in insect chemical communication, Cell. Mol. Life Sci. 63 (in press.)
11. Wetzel, C. H., Behrendt, H. J., Gisselmann, G., Stortkuhl, K. F., Hovemann, B., and Hatt, H. (2001) Functional expression and characterization of a Drosophila odorant receptor in a heterologous cell system, Proc. Natl. Acad. Sci. U.S.A. 98, 9377-9380.
12. Hallem, E. A., Fox, A. N., Zwiebel, L. J., and Carlson, J. R. (2004) Olfaction: mosquito receptor for human-sweat odorant, Nature 427, 212-213.
13. Xu, P., Atkinson, R., Jones, D. N., and Smith, D. P. (2005) Drosophila OBP LUSH is required for activity of pheromone-sensitive neurons, Neuron 45, 193-200.
14. Klein, U. (1987) Sensillum-lymph proteins from antennal olfactory hairs of the moth Antheraea polyphemus (Saturniidae), Insect Biochem. 17, 1193-1204.
15. Lee, D., Damberger, F. F., Peng, G., Horst, R., Guntert, P., Nikonova, L., Leal, W. S., and Wüthrich, K. (2002) NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH, FEBS Lett. 531, 314-318.
16. Sandler, B. H., Nikonova, L., Leal, W. S., and Clardy, J. (2000) Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein- bombykol complex, Chem. Biol. 7, 143-151.
17. Horst, R., Damberger, F., Luginbuhl, P., Guntert, P., Peng, G., Nikonova, L., Leal, W. S., and Wüthrich K. (2001) NMR structure reveals intramolecular regulation mechanism for pheromone binding and release, Proc. Natl. Acad. Sci. U.S.A. 98, 14374-14379.
18. Lartigue, A., Gruez, A., Spinelli, S., Riviere, S., Brossut, R., Tegoni, M., and Cambillau, C. (2003) The crystal structure of a cockroach pheromone-binding protein suggests a new ligand binding and release mechanism, J. Biol. Chem. 278, 30213-30218.
19. Kruse, S. W., Zhao, R., Smith, D. P., and Jones, D. N. (2003) Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster, Nat. Struct. Biol. 10, 694-700.
20. Mohanty, S., Zubkov, S., and Gronenborn, A. M. (2004) The solution NMR structure of Antheraea polyphemus PBP provides new insight into pheromone recognition by pheromone-binding proteins, J. Mol. Biol. 337, 443-451.
21. Lartigue, A., Gruez, A., Briand, L., Blon, F., Bezirard, V., Walsh, M., Pernollet, J. C., Tegoni, M., and Cambillau, C. (2004) Sulfur single wavelength anomalous diffraction crystal structure of a pheromone-binding protein from the honeybee Apis mellifera L., J. Biol. Chem. 279, 4459-4464.
22. Wogulis, M., Morgan, T., Ishida Y., Leal, W. S., and Wilson, D. K. (2005) The crystal structure of an odorant binding protein from Anopheles gambiae: Evidence for a common ligand release mechanism, Biochem. Biophys. Res. Commun. 339, 157-164.
23. Zubkov, S., Gronenborn, A. M., Byeon, I. J., and Mohanty, S. (2005) Structural consequences of the pH-induced conformational switch in A. polyphemus pheromone-binding protein: mechanisms of ligand release, J. Mol. Biol. 354, 1081-1090.
24. Mosbah, A., Campanacci, V., Lartigue, A., Tegoni, M., Cambillau, C., and Darbon, H. (2003) Solution structure of a chemosensory protein from the moth Mamestra brassicae, Biochem. J. 369, 39-44.
25. Lartigue, A., Campanacci, V., Roussel, A., Larsson, A. M., Jones, T. A., Tegoni, M., and Cambillau, C. (2002) X-ray structure and ligand binding study of a moth chemosensory protein, J. Biol. Chem. 277, 32094-32098.
26. Campanacci, V., Lartigue, A., Hallberg, B. M., Jones, T. A., Giudici-Orticoni, M. T., Tegoni, M., and Cambillau, C. (2003) Moth chemosensory protein exhibits drastic conformational changes and cooperativity on ligand binding, Proc. Natl. Acad. Sci. U.S.A. 100, 5069-5074.
27. Calvello, M., Guerra, N., Brandazza, A., D'Ambrosio, C., Scaloni, A., Dani, F. R., Turillazzi, S., and Pelosi, P. (2003) Soluble proteins of chemical communication in the social wasp Polistes dominulu, Cell. Mol. Life Sci. 60, 1933-1943.
28. Ban, L. P., Scaloni, A., Brandazza, A., Angeli, S., Zhang, L., Yan, Y. H., and Pelosi, P. (2003). Chemosensory proteins of Locusta migratoria, Insect Mol. Biol. 12, 125-134.
29. Angeli, S., Ceron, F., Scaloni, A., Monti, M., Monteforti, G., Minnocci, A., Petacchi, R., and Pelosi P. (1999) Purification, structural characterization, cloning and immunocytochemical localization of chemoreception proteins from Schistocerca gregaria, Eur. J. Biochem. 262, 745-754.
30. Picone, D., Crescenzi, O., Angeli, S., Marchese, S., Brandazza, A., Ferrara, L., Pelosi, P., and Scaloni, A. (2001) Bacterial expression and conformational analysis of a chemosensory protein from Schistocerca gregaria, Eur. J. Biochem. 268, 4794-4801.
31. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
32. Johnson, B. A., and Blevins, R. A. (1994) NMRView: A computer program for the visualization and analysis of NMR data, J. Biomol. NMR 4, 603-614.
33. Kay, L. E., Ikura, M., Tschudin, R., and Bax, A. (1990) Three-dimensional triple-resonance spectroscopy of isotopically enriched proteins, J. Magn. Reson. 89, 496-514.
34. Wittekind, M., and Mueller, L. (1993) HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins, J. Magn. Reson. B 101, 201-205.
35. Grzesieck, S., and Bax, A. (1992) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR, J. Am. Chem. Soc. 114, 6291-6293.
36. 2O samples of proteins, J. Magn. Reson. 101, 333-337.
37. Hilty, C., Wider, G., Fernandez, C., and Wüthrich, K. (2003) Stereospecific assignments of the isopropyl methyl group of the membrane protein OmpX in DHPC micelles, J. Biomol. NMR 27, 377-382.
38. Bax, A., Vuister, G. W., Grzesiek, S., Delaglio, F., Wang, A. C., Tschudin, R., and Zhu, G. (1994) Measurement of homo- and heteronuclear J couplings from quantitative J correlation, Methods Enzymol. 239, 79-105.
39. Güntert, P., Mumenthaler, C., and Wüthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA, J. Mol. Biol. 273, 283-298.
40. Güntert, P. (2003) Automated NMR protein structure calculation, Prog. NMR Spectrosc. 43, 105-125.
41. Wang, J., Cieplak, P., and Kollman, P. A. (2000) How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules, J. Comput. Chem. 24, 1999-2012.
42. Hawkins, G. D., Cramer, C. J., and Truhlar, D. G. (1995) Pairwise solute screening of solute charges from a dielectric medium, Chem. Phys. Lett. 246, 122-129.
43. Hawkins, G. D., Cramer, C. J., and Truhlar, D. G. (1996) Parameterized models of aqueous free energies of solvation based on pairwise descreening of solute atomic charges from a dielectric medium, J. Phys. Chem. 100, 19824-19839.
44. Laskowski, R. A., Rullmann, J. A. C., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR, J. Biomol. NMR 8, 477-486.
45. Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.
46. Binkowski, T. A., Naghibzadeh, S., and Liang, J. (2003) CASTp: Computed atlas of surface topography of proteins, Nucleic Acids Res. 31, 3352-3355.
47. Liang, J., Edelsbrunner, H., and Woodward, C. (1998) Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design, Protein Sci. 7, 1884-1897.
48. Dorman, E. D., and Bovey, F. A. (1973) Proton coupled carbon-13 magnetic resonance spectra. The simple amides, J. Org. Chem. 38, 2379-2383.
49. Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology, J. Biomol. NMR 13, 289-302.
50. Frishman, D., and Argos, P. (1995) Knowledge-based secondary structure assignment, Proteins 23, 566-579.
51. Hutchinson, E. G., and Thornton, J. M. (1996) PROMOTIF-A program to identify and analyze structural motifs in proteins, Protein Sci. 5, 212-220.
52. Ban, L. P., Zhang, L., Yan, Y. H., and Pelosi, P. (2002) Binding properties of a locust's chemosensory protein, Biochem. Biophys. Res. Commun. 293, 50-54.
53. Tegoni, M., Campanacci, V., and Cambillau, C. (2004) Structural aspects of sexual attraction and chemical communication in insects, Trends Biochem. Sci. 29, 257-264.
54. Ban, L. P., Scaloni, A., D'Ambrosio, C., Zhang, L., Yan, Y. H., and Pelosi, P. (2003) Biochemical characterisation and bacterial expression of an odorant-binding protein from Locusta migratoria, Cell. Mol. Life Sci. 60, 390-400.
55. Pelosi, P. (2001) The role of perireceptor events in vertebrate olfaction, Cell. Mol. Life Sci. 58, 503-509.