1GT5

Complexe of Bovine Odorant Binding Protein with benzophenone

Summary for 1GT5

• Entry DOI: 10.2210/pdb1gt5/pdb
• Related: 1G85 1GT1 1GT3 1GT4 1HN2 1OBP 1PBO
• Descriptor: ODORANT-BINDING PROTEIN, DIPHENYLMETHANONE (3 entities in total)
• Functional Keywords: lipocalin, bovine odorant binding protein
• Biological source: BOS TAURUS (BOVINE)
• Cellular location: Secreted: P07435
• Total number of polymer chains: 2
• Total formula weight: 37421.20

Authors

Vincent, F.,Ramoni, R.,Spinelli, S.,Grolli, S.,Conti, V.,Cambillau, C.,Tegoni, M. (deposition date: 2002-01-10, release date: 2003-10-03, Last modification date: 2023-12-13)

Primary citation

Vincent, F.,Ramoni, R.,Spinelli, S.,Grolli, S.,Tegoni, M.,Cambillau, C.
Crystal Structures of Bovine Odorant-Binding Protein in Complex with Odorant Molecules.
Eur.J.Biochem., 271:3832-, 2004

PubMed Abstract: The structure of bovine odorant-binding protein (bOBP) revealed a striking feature of a dimer formed by domain swapping [Tegoni, M., Ramoni, R., Bignetti, E., Spinelli, S. & Cambillau, C. (1996) Nat. Struct. Biol.3, 863-867; Bianchet, M.A., Bains, G., Pelosi, P., Pevsner, J., Snyder, S.H., Monaco, H.L. & Amzel, L.M. (1996) Nat. Struct. Biol.3, 934-939] and the presence of a naturally occuring ligand [Ramoni, R., Vincent, F., Grolli, S., Conti, V., Malosse, C., Boyer, F.D., Nagnan-Le Meillour, P., Spinelli, S., Cambillau, C. & Tegoni, M. (2001) J. Biol. Chem.276, 7150-7155]. These features led us to investigate the binding of odorant molecules with bOBP in solution and in the crystal. The behavior of odorant molecules in bOBP resembles that observed with porcine OBP (pOBP), although the latter is monomeric and devoid of ligand when purified. The odorant molecules presented K(d) values with bOBP in the micromolar range. Most of the X-ray structures revealed that odorant molecules interact with a common set of residues forming the cavity wall and do not exhibit specific interactions. Depending on the ligand and on the monomer (A or B), a single residue--Phe89--presents alternate conformations and might control cross-talking between the subunits. Crystal data on both pOBP and bOBP, in contrast with binding and spectroscopic studies on rat OBP in solution, reveal an absence of significant conformational changes involving protein loops or backbone. Thus, the role of OBP in signal triggering remains unresolved.

PubMed: 15373829
DOI: 10.1111/J.1432-1033.2004.04315.X

Experimental method

X-RAY DIFFRACTION (2.08 Å)