5thm: Difference between revisions

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<StructureSection load='5thm' size='340' side='right'caption='[[5thm]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='5thm' size='340' side='right'caption='[[5thm]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5thm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5THM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5THM FirstGlance]. <br>
<table><tr><td colspan='2'>[[5thm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5THM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5THM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7BZ:N,N-DIMETHYLBORANAMINE'>7BZ</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7BZ:N,N-DIMETHYLBORANAMINE'>7BZ</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </span></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=5thm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5thm OCA], [https://pdbe.org/5thm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5thm RCSB], [https://www.ebi.ac.uk/pdbsum/5thm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5thm ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5thm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5thm OCA], [http://pdbe.org/5thm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5thm RCSB], [http://www.ebi.ac.uk/pdbsum/5thm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5thm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/EST6_DROME EST6_DROME]] Transferred from the ejaculatory bulbs of males to the female genitals upon copulation, plays an important role in the reproductive biology.  
[https://www.uniprot.org/uniprot/EST6_DROME EST6_DROME] Transferred from the ejaculatory bulbs of males to the female genitals upon copulation, plays an important role in the reproductive biology.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Carboxylesterase]]
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Fraser, N J]]
[[Category: Fraser NJ]]
[[Category: Jackson, C J]]
[[Category: Jackson CJ]]
[[Category: Hydrolase]]

Latest revision as of 16:01, 4 October 2023

Esterase-6 from Drosophila melanogasterEsterase-6 from Drosophila melanogaster

Structural highlights

5thm is a 1 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EST6_DROME Transferred from the ejaculatory bulbs of males to the female genitals upon copulation, plays an important role in the reproductive biology.

Publication Abstract from PubMed

Previous electrophysiological and behavioural studies implicate esterase 6 in the processing of the pheromone cis-vaccenyl acetate and various food odorants that affect aggregation and reproductive behaviours. Here we show esterase 6 has relatively high activity against many of the short-mid chain food esters, but negligible activity against cis-vaccenyl acetate. The crystal structure of esterase 6 confirms its substrate-binding site can accommodate many short-mid chain food esters but not cis-vaccenyl acetate. Immunohistochemical assays show esterase 6 is expressed in non-neuronal cells in the third antennal segment that could be accessory or epidermal cells surrounding numerous olfactory sensilla, including basiconics involved in food odorant detection. Esterase 6 is also produced in trichoid sensilla, but not in the same cell types as the cis-vaccenyl acetate binding protein LUSH. Our data support a model in which esterase 6 acts as a direct odorant degrading enzyme for many bioactive food esters, but not cis-vaccenyl acetate.

Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila.,Younus F, Fraser NJ, Coppin CW, Liu JW, Correy GJ, Chertemps T, Pandey G, Maibeche M, Jackson CJ, Oakeshott JG Sci Rep. 2017 Apr 10;7:46188. doi: 10.1038/srep46188. PMID:28393888[1]

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

See Also

References

  1. Younus F, Fraser NJ, Coppin CW, Liu JW, Correy GJ, Chertemps T, Pandey G, Maibeche M, Jackson CJ, Oakeshott JG. Molecular basis for the behavioral effects of the odorant degrading enzyme Esterase 6 in Drosophila. Sci Rep. 2017 Apr 10;7:46188. doi: 10.1038/srep46188. PMID:28393888 doi:http://dx.doi.org/10.1038/srep46188

5thm, resolution 2.15Å

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