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==SOLUTION STRUCTURE OF DROSOMYCIN, THE FIRST INDUCIBLE ANTIFUNGAL PROTEIN FROM INSECTS, NMR, 15 STRUCTURES== | ==SOLUTION STRUCTURE OF DROSOMYCIN, THE FIRST INDUCIBLE ANTIFUNGAL PROTEIN FROM INSECTS, NMR, 15 STRUCTURES== | ||
<StructureSection load='1myn' size='340' side='right' caption='[[1myn | <StructureSection load='1myn' size='340' side='right'caption='[[1myn]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1myn]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1myn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MYN FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 models</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=1myn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myn OCA], [https://pdbe.org/1myn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1myn RCSB], [https://www.ebi.ac.uk/pdbsum/1myn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1myn ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/DMYC_DROME DMYC_DROME] Possesses antifungal activity and is active against a relatively broad spectrum of filamentous fungi. It inhibits spore germination at high concentrations and at low concentrations delays growth of hyphae which subsequently exhibit abnormal morphology. Spz C-106 in the hemolymph controls expression of the antifungal peptide by acting as a ligand of Tl and inducing an intracellular signaling pathway.<ref>PMID:8808632</ref> <ref>PMID:12872120</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/my/1myn_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/my/1myn_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1myn ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 25: | Line 27: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1myn" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 30: | Line 33: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Hetru | [[Category: Large Structures]] | ||
[[Category: Hoffmann | [[Category: Hetru C]] | ||
[[Category: Landon | [[Category: Hoffmann JA]] | ||
[[Category: Ptak | [[Category: Landon C]] | ||
[[Category: Sodano | [[Category: Ptak M]] | ||
[[Category: Sodano P]] | |||
Latest revision as of 03:16, 21 November 2024
SOLUTION STRUCTURE OF DROSOMYCIN, THE FIRST INDUCIBLE ANTIFUNGAL PROTEIN FROM INSECTS, NMR, 15 STRUCTURESSOLUTION STRUCTURE OF DROSOMYCIN, THE FIRST INDUCIBLE ANTIFUNGAL PROTEIN FROM INSECTS, NMR, 15 STRUCTURES
Structural highlights
FunctionDMYC_DROME Possesses antifungal activity and is active against a relatively broad spectrum of filamentous fungi. It inhibits spore germination at high concentrations and at low concentrations delays growth of hyphae which subsequently exhibit abnormal morphology. Spz C-106 in the hemolymph controls expression of the antifungal peptide by acting as a ligand of Tl and inducing an intracellular signaling pathway.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDrosomycin is the first antifungal protein characterized recently among the broad family of inducible peptides and proteins produced by insects to respond to bacterial or septic injuries. It is a small protein of 44 amino acid residues extracted from Drosophila melanogaster that exhibits a potent activity against filamentous fungi. Its three-dimensional structure in aqueous solution was determined using 1H 2D NMR. This structure, involving an alpha-helix and a twisted three-stranded beta-sheet, is stabilized by three disulfide bridges. The corresponding Cysteine Stabilized alpha beta (CS alpha beta) motif, which was found in other defense proteins such as the antibacterial insect defensin A, short- and long-chain scorpion toxins, as well as in plant thionins and potent antifungal plant defensins, appears as remarkably persistent along evolution. Solution structure of drosomycin, the first inducible antifungal protein from insects.,Landon C, Sodano P, Hetru C, Hoffmann J, Ptak M Protein Sci. 1997 Sep;6(9):1878-84. PMID:9300487[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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