6hhe

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Crystal structure of the medfly Odorant Binding Protein CcapOBP22/CcapOBP69aCrystal structure of the medfly Odorant Binding Protein CcapOBP22/CcapOBP69a

Structural highlights

6hhe is a 1 chain structure with sequence from Cerca. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:OBP69a (CERCA)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

In insects, odorant-binding proteins (OBPs) connect the peripheral sensory system to receptors of olfactory organs. Medfly Ceratitis capitata CcapObp22 shows 37% identity and close phylogenetic affinities with Drosophila melanogaster OBP69a/PB-PRP1 (pheromone-binding protein related protein 1). The CcapObp22 gene is transcribed in the antennae and maxillary palps, suggesting an active role in olfaction. Here, we recombinantly produced CcapObp22, obtaining a 13.5 kDa protein capable of binding multiple strongly hydrophobic terpene compounds, including medfly male pheromone components. The highest binding affinity (EC50 0.48 muM) was to (E,E)-alpha-farnesene, one of the most abundant compounds in the male pheromone blend. This odorant was used in co-crystallization experiments, yielding the structure of CcapOBP22. The monomeric structure shows the typical OBP folding, constituted by six alpha-helical elements interconnected by three disulfide bridges. A C-terminal seventh alpha-helix constitutes the wall of a deep, L-shaped hydrophobic cavity. Analysis of the electron density in this cavity suggested trapping of farnesene in the crystal structure, although with partial occupancy. Superposition of the CcapOBP22 structure with related 7-helical OBPs highlights striking similarity in the organization of the C-terminal segment of these proteins. Collectively, our molecular and physiological data on medfly CcapOBP22 suggest its involvement in inter-sex olfactory communication. This article is protected by copyright. All rights reserved.

Structural and biochemical evaluation of Ceratitis capitata OBP22 affinity for odorants involved in inter-sex communication.,Falchetto M, Ciossani G, Scolari F, Di Cosimo A, Nenci S, Field LM, Mattevi A, Zhou JJ, Gasperi G, Forneris F Insect Mol Biol. 2018 Dec 12. doi: 10.1111/imb.12559. PMID:30548711[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Falchetto M, Ciossani G, Scolari F, Di Cosimo A, Nenci S, Field LM, Mattevi A, Zhou JJ, Gasperi G, Forneris F. Structural and biochemical evaluation of Ceratitis capitata OBP22 affinity for odorants involved in inter-sex communication. Insect Mol Biol. 2018 Dec 12. doi: 10.1111/imb.12559. PMID:30548711 doi:http://dx.doi.org/10.1111/imb.12559

6hhe, resolution 1.52Å

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