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1G85

CRYSTAL STRUCTURE OF BOVINE ODORANT BINDING PROTEIN COMPLEXED WITH IS NATURAL LIGAND

Summary for 1G85
Entry DOI10.2210/pdb1g85/pdb
Related1OBP
DescriptorODORANT-BINDING PROTEIN, (3R)-oct-1-en-3-ol (3 entities in total)
Functional Keywordslipocalin, swapping domain, homodimer, signaling protein
Biological sourceBos taurus (cattle)
Cellular locationSecreted: P07435
Total number of polymer chains2
Total formula weight37425.48
Authors
Vincent, F.,Spinelli, S.,Cambillau, C.,Tegoni, M. (deposition date: 2000-11-16, release date: 2002-06-26, Last modification date: 2023-08-09)
Primary citationRamoni, R.,Vincent, F.,Grolli, S.,Conti, V.,Malosse, C.,Boyer, F.D.,Nagnan-Le Meillour, P.,Spinelli, S.,Cambillau, C.,Tegoni, M.
The insect attractant 1-octen-3-ol is the natural ligand of bovine odorant-binding protein.
J.Biol.Chem., 276:7150-7155, 2001
Cited by
PubMed Abstract: Bovine odorant-binding protein (bOBP) is a dimeric lipocalin present in large amounts in the respiratory and olfactory nasal mucosa. The structure of bOBP refined at 2.0-A resolution revealed an elongated volume of electron density inside each buried cavity, indicating the presence of one (or several) naturally occurring copurified ligand(s) (Tegoni et al. (1996) Nat. Struct. Biol. 3, 863-867; Bianchet et al. (1996) Nat. Struct. Biol. 3, 934-939). In the present work, by combining mass spectrometry, x-ray crystallography (1.8-A resolution), and fluorescence, it has been unambiguously established that natural bOBP contains the racemic form of 1-octen-3-ol. This volatile substance is a typical component of bovine breath and in general of odorous body emanations of humans and animals. The compound 1-octen-3-ol is also an extremely potent olfactory attractant for many insect species, including some parasite vectors like Anopheles (Plasmodium) or Glossina (Trypanosoma). For the first time, a function can be assigned to an OBP, with a possible role of bOBP in the ecological relationships between bovine and insect species.
PubMed: 11114310
DOI: 10.1074/jbc.M010368200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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