Abstract
Odorant binding protein (OBP) is the major odorant binding component of mammalian nasal mucosa. The two structures of bovine OBP reported in this paper (one crystallized as purified and one soaked in the presence of a selenium-containing odorant) show that: (i) the OBP dimer is composed of two compact domains related by an approximate two-fold axis of symmetry; (ii) between residues 122 and 123 the polypeptide chains cross from one domain to the other such that each domain is formed by residues from both monomers; (iii) purified OBP already contains two bound odorant molecules (one per monomer)—odorant binding occurs by replacement of these molecules with the added odorant; and (iv) the structure of the odorant binding site can explain OBP's extraordinarily broad odorant specificity.
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References
Pelosi, P. Odorant binding proteins. Crit. Rev. Biochem. Molec. Biol. 29, 199–228 (1994).
Snyder, S.H., Sklar, P.B. & Pevsner, J. Molecular mechanisms of olfaction. J. Biol. Chem. 263, 13971–13974 (1988).
Pevsner, J., Reed, R.R., Feinstein, P.G. & Snyder, S.H. Molecular cloning of odorant-binding protein: member of a ligand carrier family. Science 241, 336–339 (1988).
Pelosi, P. & Tirindelli, R. Structure/activity studies and characterization of an odorant-binding protein. In: Chemical Senses, Vol 1. Receptor Events and Transduction in Taste and Olfaction. (Eds J.G. Brand, J.H. Teeter, R.H. Cagan, & M.R. Kare) 207–225 (Marcel Dekker, New York, 1989).
Pevsner, J., Hou, V., Snowman, A.M. & Snyder, S.H. Odorant-binding protein, characterization of ligand binding. J. Biol. Chem. 265, 6118–6125 (1990).
Tirindelli, R., Keen, N.J., Cavaggioni, A., Eliopoulos, E.E. & Findlay, J.B.C. Complete amino acid sequence of pyrazine-binding protein from cow nasal mucosa. Eur. J. Biochem. 185, 569–572 (1989).
Cowan, S.W., Newcomer, M.E. & Jones, T.A. Crystallographic refinement of human serum retinol binding protein at 2 Å resolution. Proteins 8, 44 (1990).
Zanotti, G., Berni, R. & Monaco, H.L. Crystal structure of liganded and unliganded forms of bovine plasma retinol-binding protein. J. Biol. Chem. 268, 10728–10738 (1993).
Papiz, M.Z. et al. The structure of β lactoglobulin and its similarity to plasma retinol-binding protein. Nature 324, 383–385 (1986).
Monaco, H.L. et al. Crystal structure of the trigonal form of bovine beta lactoglobulin and of its complex with retinol at 2.5 A resolution. J. Mol. Biol. 197, 695–706 (1987).
Holden, H.M., Rypniewski, W.R., Law, J.H. & Rayment, I. The molecular structure of insecticyanin from tobacco hornworm Manduca sexta L. at 2.6 A resolution. EMBO J. 6, 1565–1570 (1987).
Huber, R. et al. Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae. J. Mol. Biol. 195, 423–134 (1987).
Huber, R. et al. Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 Å resolution. J. Mol. Biol. 198, 499–513 (1987).
Bocskel, Z. et al. Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography. Nature 360, 186–188 (1992).
Bennett, M.J., Schlunegger, M.P. & Eisenberg, D. 3D Domain swapping: A mechanism for oligomer assembly. Prot. Sci. 4, 2455–2468 (1995).
Green, S.M., Gittis, A.G., Meeker, A.K. & Lattman, E.E. One-step evolution of a dimerfrom a monomeric protein. Nature Struct. Biol. 2, 746–751 (1995).
Monaco, H.L. & Zanotti, G. The three dimensional structure of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity. Biopolymers 32, 457–465 (1992).
Janin, J. Elusive affinities. Proteins Struct. Funct. Genet. 21, 30–39 (1995).
Murphy, K.P., Xie, D., Thompson, K.S., Amzel, L.M. & Freire, E. Entropy in biological binding processes: Estimation of translational entropy loss. Proteins Struct. Funct. Genet. 18, 63–67 (1994).
Bussolati, L., Ramoni, R., Grolli, S., Donofrio, G. & Bignetti, E. Preparation of an affinity resin for odorant by coupling odorant binding protein from bovine nasal mucosa to Sepharose 4B. J. Biotech. 30, 225–230 (1993).
Napolitano, E. & Pelosi, P. Synthesis of thiazole and selenazole derivatives with affinity for the odorant-binding protein. Biorg. Medic. Chem. Letts. 2, 1603–1606 (1992).
Pevsner, J., Trifiletti, R.R., Strittmatter, S.M. & Snyder, S.H. Isolation and characterization of an olfactory receptor protein for odorant pyrazynes. Proc. Natl. Acad. Sci. USA 82, 3050–3054 (1985).
Sivaprasadarao, A. & Findlay, J.B.C. The interaction of retinol-binding protein with its plasma-membrane receptor. Biochem. J. 255, 561–569 (1988).
Bavik, C.O., Levy, F., Wernstedt, C. & Ericksson, U. The retinol pigment epithelial membrane receptor for plasma retinol-binding protein. J. Biol. Chem. 268, 20540–20546 (1993).
Boudjelal, M., Sivaprasadarao, A. & Findlay, J.B.C. Membrane receptor for odour-binding proteins. Biochem. J. 317, 23–27 (1996).
Zeng, C. et al. A human azillary odorant is carried by apolipoprotein D. Proc. Natl. Acad. Sci. 93, 6626–6630 (1996).
Reed, R.R. The molecular basis of sensitivity and specificity in olfaction. Sem. Cell Biol. 5, 33–38 (1994).
Kleywegt, G.J. & Jones, T.A. Detection, delineation, measurement and display of cavities in proteins. Acta Crystallogr. D50, 178–185 (1994).
Collaborative Computational Project Number 4. Acta Crystallogr. D50, 760–767 (1994).
Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjelgaard, M. Improved methods for building protein models in electron density maps and location of errors in these maps. Acta Crystallogr. A47, 110–119 (1991).
Brünger, A.T. X-PLOK. A system for crystallography and NMR, 3.1 Manual. Yale Univ. Press, New Haven, CT (1992).
Nicholls, A., Sharp, K. & Honig, B. GRASP: Graphical representation and analysis of structural properties of proteins. Proteins 11, 281–296 (1991).
Tegoni, M., Ramoni, R., Bignetti, E., Spinelli, S. & Cambillau, C. Domain swapping creates a third putative combining site in bovine odorant binding protein dimer. Nature Struct. Biol. 3, 863–867 (1996).
Evans, S.V. SETOR: Hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics 11, 134–138 (1993).
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Bianchet, M., Bains, G., Pelosi, P. et al. The three-dimensional structure of bovine odorant binding protein and its mechanism of odor recognition. Nat Struct Mol Biol 3, 934–939 (1996). https://doi.org/10.1038/nsb1196-934
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DOI: https://doi.org/10.1038/nsb1196-934
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