7uo6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
The | ==NMR structure of Pheromone-binding protein 2 in Ostrinia furnacalis== | ||
<StructureSection load='7uo6' size='340' side='right'caption='[[7uo6]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7uo6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ostrinia_furnacalis Ostrinia furnacalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UO6 FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7uo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uo6 OCA], [https://pdbe.org/7uo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uo6 RCSB], [https://www.ebi.ac.uk/pdbsum/7uo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uo6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/E7CCA0_OSTFU E7CCA0_OSTFU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ostrinia furnacalis is an invasive lepidopteran agricultural pest that relies on olfaction for mating and reproduction. Male moths have an extremely sensitive olfactory system that can detect the sex pheromones emitted by females over a great distance. Pheromone-binding proteins present in the male moth antenna play a key role in the pheromone uptake, transport, and release at the dendritic membrane of the olfactory neuron. Here, we report the first high-resolution NMR structure of a pheromone-binding protein from an Ostrinia species at pH 6.5. The core of the Ostrinia furnacalis PBP2 (OfurPBP2) consists of six helices, alpha1a (2-14), alpha1b (16-22), alpha2 (27-37), alpha3 (46-60), alpha4 (70-80), alpha5 (84-100), and alpha6 (107-124) surrounding a large hydrophobic pocket. The structure is stabilized by three disulfide bridges, 19-54, 50-108, and 97-117. In contrast to the unstructured C-terminus of other lepidopteran PBPs, the C-terminus of OfurPBP2 folds into an alpha-helix (alpha7) at pH 6.5. The protein has nanomolar affinity towards both pheromone isomers. Molecular docking of both pheromones, E-12 and Z-12-tetradecenyl acetate, to OfurPBP2 revealed that the residues Met5, Lys6, Met8, Thr9, Phe12, Phe36, Trp37, Phe76, Ser115, Phe118, Lys119, Ile122, His123, and Ala128 interact with both isomers, while Thr9 formed a hydrogen bond with the acetate head group. NMR structure and thermal unfolding studies with CD suggest that ligand release at pH 4.5 is likely due to the partial unfolding of the protein. | |||
Ostrinia furnacalis PBP2 solution NMR structure: Insight into ligand binding and release mechanisms.,Dahal SR, Lewellen JL, Ayyappan S, Chaudhary BP, Nukala V, Mohanty S Protein Sci. 2022 Oct;31(10):e4438. doi: 10.1002/pro.4438. PMID:36173163<ref>PMID:36173163</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7uo6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Ostrinia furnacalis]] | |||
[[Category: Ayyappan S]] | |||
[[Category: Mohanty S]] | |||
Revision as of 13:22, 15 February 2023
NMR structure of Pheromone-binding protein 2 in Ostrinia furnacalisNMR structure of Pheromone-binding protein 2 in Ostrinia furnacalis
Structural highlights
FunctionPublication Abstract from PubMedOstrinia furnacalis is an invasive lepidopteran agricultural pest that relies on olfaction for mating and reproduction. Male moths have an extremely sensitive olfactory system that can detect the sex pheromones emitted by females over a great distance. Pheromone-binding proteins present in the male moth antenna play a key role in the pheromone uptake, transport, and release at the dendritic membrane of the olfactory neuron. Here, we report the first high-resolution NMR structure of a pheromone-binding protein from an Ostrinia species at pH 6.5. The core of the Ostrinia furnacalis PBP2 (OfurPBP2) consists of six helices, alpha1a (2-14), alpha1b (16-22), alpha2 (27-37), alpha3 (46-60), alpha4 (70-80), alpha5 (84-100), and alpha6 (107-124) surrounding a large hydrophobic pocket. The structure is stabilized by three disulfide bridges, 19-54, 50-108, and 97-117. In contrast to the unstructured C-terminus of other lepidopteran PBPs, the C-terminus of OfurPBP2 folds into an alpha-helix (alpha7) at pH 6.5. The protein has nanomolar affinity towards both pheromone isomers. Molecular docking of both pheromones, E-12 and Z-12-tetradecenyl acetate, to OfurPBP2 revealed that the residues Met5, Lys6, Met8, Thr9, Phe12, Phe36, Trp37, Phe76, Ser115, Phe118, Lys119, Ile122, His123, and Ala128 interact with both isomers, while Thr9 formed a hydrogen bond with the acetate head group. NMR structure and thermal unfolding studies with CD suggest that ligand release at pH 4.5 is likely due to the partial unfolding of the protein. Ostrinia furnacalis PBP2 solution NMR structure: Insight into ligand binding and release mechanisms.,Dahal SR, Lewellen JL, Ayyappan S, Chaudhary BP, Nukala V, Mohanty S Protein Sci. 2022 Oct;31(10):e4438. doi: 10.1002/pro.4438. PMID:36173163[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||