PDBsum entry 1a3y

Lipocalin

PDB id

1a3y

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Contents

			Protein chains

					149 a.a. *

			Waters ×561

* Residue conservation analysis

PDB id:

1a3y

Links

Name:

Lipocalin

Title:

Odorant binding protein from nasal mucosa of pig

Structure:

Odorant binding protein. Chain: a, b

Source:

Sus scrofa. Pig. Organism_taxid: 9823. Organ: nose. Tissue: olfactory epithelium

Resolution:

2.25Å

R-factor:

0.181

R-free:

0.247

Authors:

S.Spinelli,C.Cambillau,M.Tegoni

Key ref:

S.Spinelli et al. (1998). The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism. Biochemistry, 37, 7913-7918. PubMed id: 9609684 DOI: 10.1021/bi980179e

Date:

27-Jan-98

Release date:

16-Feb-99

PROCHECK

	Headers

	References

Protein chains

P81245 (OBP_PIG) - Odorant-binding protein from Sus scrofa

Seq: Struc:					157 a.a. 149 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

DOI no: 10.1021/bi980179e	Biochemistry 37:7913-7918 (1998)
PubMed id: 9609684

The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism.
S.Spinelli, R.Ramoni, S.Grolli, J.Bonicel, C.Cambillau, M.Tegoni.

ABSTRACT

The X-ray structure of the porcine odorant binding protein (OBPp) was determined at 2.25 A resolution. This lipocalin is a monomer and is devoid of naturally occurring bound ligand, contrary to what was observed in the case of bovine OBP [Tegoni, M., et al. (1996) Nat. Struct. Biol. 3, 863-867; Bianchet, M. A., et al. (1996) Nat. Struct. Biol. 3, 934-939]. In this latter protein, a dimer without any disulfide bridges, domain swapping was found to occur between the beta- and alpha-domains. A single Gly (121) insertion was found in OBPp when it was compared to OBPb, which may prevent domain swapping from taking place. The presence of a disulfide bridge between the OBPp beta- and alpha-domains (cysteines 63 and 155) may lock the resulting fold in a nonswapped monomeric conformation. Comparisons with other OBPs indicate that the two cysteines involved in the OBPp disulfide bridge are conserved in the sequence, suggesting that OBPp may be considered a prototypic OBP fold, and not OBPb.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20352304

D.Kmiecik, and J.R.Albani (2010).
Effect of 1-aminoanthracene (1-AMA) binding on the structure of three lipocalin proteins, the dimeric β lactoglobulin, the dimeric odorant binding protein and the monomeric α1-acid glycoprotein. Fluorescence spectra and lifetimes studies.

J Fluoresc, 20, 973-983.

20589419

F.Brimau, J.P.Cornard, C.Le Danvic, P.Lagant, G.Vergoten, D.Grebert, E.Pajot, and P.Nagnan-Le Meillour (2010).
Binding specificity of recombinant odorant-binding protein isoforms is driven by phosphorylation.

J Chem Ecol, 36, 801-813.

20545700

L.Mattsson, T.Lundgren, P.Olsson, M.Sundberg, and J.Lidholm (2010).
Molecular and immunological characterization of Can f 4: a dog dander allergen cross-reactive with a 23 kDa odorant-binding protein in cow dander.

Clin Exp Allergy, 40, 1276-1287.

19390145

S.A.White, L.Briand, D.J.Scott, and A.J.Borysik (2009).
Structure of rat odorant-binding protein OBP1 at 1.6 A resolution.

Acta Crystallogr D Biol Crystallogr, 65, 403-410.

PDB code:

3fiq

18260099

A.Marabotti, T.Lefèvre, M.Staiano, R.Crescenzo, A.Varriale, M.Rossi, M.Pézolet, and S.D'Auria (2008).
Mutant bovine odorant-binding protein: Temperature affects the protein stability and dynamics as revealed by infrared spectroscopy and molecular dynamics simulations.

Proteins, 72, 769-778.

18190694

B.Adam, B.Charloteaux, J.Beaufays, L.Vanhamme, E.Godfroid, R.Brasseur, and L.Lins (2008).
Distantly related lipocalins share two conserved clusters of hydrophobic residues: use in homology modeling.

BMC Struct Biol, 8, 1.

18098179

M.Staiano, M.Saviano, P.Herman, Z.Grycznyski, C.Fini, A.Varriale, A.Parracino, A.B.Kold, M.Rossi, and S.D'Auria (2008).
Time-resolved fluorescence spectroscopy and molecular dynamics simulations point out the effects of pressure on the stability and dynamics of the porcine odorant-binding protein.

Biopolymers, 89, 284-291.

17918730

O.V.Stepanenko, A.Marabotti, I.M.Kuznetsova, K.K.Turoverov, C.Fini, A.Varriale, M.Staiano, M.Rossi, and S.D'Auria (2008).
Hydrophobic interactions and ionic networks play an important role in thermal stability and denaturation mechanism of the porcine odorant-binding protein.

Proteins, 71, 35-44.

17393279

W.M.Xiu, and S.L.Dong (2007).
Molecular characterization of two pheromone binding proteins and quantitative analysis of their expression in the beet armyworm, Spodoptera exigua Hübner.

J Chem Ecol, 33, 947-961.

16849331

E.Hajjar, D.Perahia, H.Débat, C.Nespoulous, and C.H.Robert (2006).
Odorant binding and conformational dynamics in the odorant-binding protein.

J Biol Chem, 281, 29929-29937.

17042783

S.Grolli, E.Merli, V.Conti, E.Scaltriti, and R.Ramoni (2006).
Odorant binding protein has the biochemical properties of a scavenger for 4-hydroxy-2-nonenal in mammalian nasal mucosa.

FEBS J, 273, 5131-5142.

15654894

J.S.Johansson, G.A.Manderson, R.Ramoni, S.Grolli, and R.G.Eckenhoff (2005).
Binding of the volatile general anesthetics halothane and isoflurane to a mammalian beta-barrel protein.

FEBS J, 272, 573-581.

15373829

F.Vincent, R.Ramoni, S.Spinelli, S.Grolli, M.Tegoni, and C.Cambillau (2004).
Crystal structures of bovine odorant-binding protein in complex with odorant molecules.

Eur J Biochem, 271, 3832-3842.

PDB codes:

1gt1 1gt3 1gt4 1gt5

11856834

F.J.Hoedemaeker, R.W.Visschers, A.C.Alting, K.G.de Kruif, M.E.Kuil, and J.P.Abrahams (2002).
A novel pH-dependent dimerization motif in beta-lactoglobulin from pig (Sus scrofa).

Acta Crystallogr D Biol Crystallogr, 58, 480-486.

PDB code:

1exs

12044155

L.Briand, C.Eloit, C.Nespoulous, V.Bézirard, J.C.Huet, C.Henry, F.Blon, D.Trotier, and J.C.Pernollet (2002).
Evidence of an odorant-binding protein in the human olfactory mucus: location, structural characterization, and odorant-binding properties.

Biochemistry, 41, 7241-7252.

11119644

M.Perduca, F.Mancia, R.Del Giorgio, and H.L.Monaco (2001).
Crystal structure of a truncated form of porcine odorant-binding protein.

Proteins, 42, 201-209.

PDB code:

1hqp

10662696

B.H.Sandler, L.Nikonova, W.S.Leal, and J.Clardy (2000).
Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein-bombykol complex.

Chem Biol, 7, 143-151.

PDB code:

1dqe

11058743

D.R.Flower, A.C.North, and C.E.Sansom (2000).
The lipocalin protein family: structural and sequence overview.

Biochim Biophys Acta, 1482, 9.

11058746

D.R.Flower (2000).
Experimentally determined lipocalin structures.

Biochim Biophys Acta, 1482, 46-56.

10913308

E.Plettner, J.Lazar, E.G.Prestwich, and G.D.Prestwich (2000).
Discrimination of pheromone enantiomers by two pheromone binding proteins from the gypsy moth Lymantria dispar.

Biochemistry, 39, 8953-8962.

10806409

L.Briand, C.Nespoulous, V.Perez, J.J.Rémy, J.C.Huet, and J.C.Pernollet (2000).
Ligand-binding properties and structural characterization of a novel rat odorant-binding protein variant.

Eur J Biochem, 267, 3079-3089.

10561587

E.Thavathiru, N.R.Jana, and P.K.De (1999).
Abundant secretory lipocalins displaying male and lactation-specific expression in adult hamster submandibular gland. cDNA cloning and sex hormone-regulated repression.

Eur J Biochem, 266, 467-476.

10209290

S.Paolini, F.Tanfani, C.Fini, E.Bertoli, and Paolo Pelosi (1999).
Porcine odorant-binding protein: structural stability and ligand affinities measured by fourier-transform infrared spectroscopy and fluorescence spectroscopy.

Biochim Biophys Acta, 1431, 179-188.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.