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2l8x
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2l8x is ON HOLD Authors: Shenkarev, Z.O., Trunov, K.I., Paramonov, A.S., Arseniev, A.S. Description: Spatial structure of antimicrobial peptide Are...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Spatial structure of antimicrobial peptide Arenicin-2 dimer in DPC micelles== | |
| + | <StructureSection load='2l8x' size='340' side='right'caption='[[2l8x]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2l8x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arenicola_marina Arenicola marina]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L8X FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 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=2l8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l8x OCA], [https://pdbe.org/2l8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l8x RCSB], [https://www.ebi.ac.uk/pdbsum/2l8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l8x ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ANN2_AREMA ANN2_AREMA] Has antimicrobial activity against the Gram-negative bacteria E.coli and P.mirabilis, the Gram-positive bacterium L.monocytogenes and the yeast C.albicans.<ref>PMID:15527787</ref> <ref>PMID:17935487</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The membrane-active, cationic, beta-hairpin peptide, arenicin, isolated from marine polychaeta Arenicola marina exhibits a broad spectrum of antimicrobial activity. The peptide in aqueous solution adopts the significantly twisted beta-hairpin conformation without pronounced amphipathicity. To assess the mechanism of arenicin action, the spatial structure and backbone dynamics of the peptide in membrane-mimicking media and its pore-forming activity in planar lipid bilayers were studied. The spatial structure of the asymmetric arenicin dimer stabilized by parallel association of N-terminal strands of two beta-hairpins was determined using triple-resonance nuclear magnetic resonance (NMR) spectroscopy in dodecylphosphocholine (DPC) micelles. Interaction of arenicin with micelles and its oligomerization significantly decreased the right-handed twist of the beta-hairpin, increased its amphipathicity, and led to stabilization of the peptide backbone on a picosecond to nanosecond time scale. Relaxation enhancement induced by water-soluble (Mn(2+)) and lipid-soluble (16-doxylstearate) paramagnetic probes pointed to the dimer transmembrane arrangement. Qualitative NMR and circular dichroism study of arenicin-2 in mixed DPC/1,2-dioleoyl-sn-glycero-3-phosphoglycerol bicelles, sodium dodecyl sulfate micelles, and lipid vesicles confirmed that a similar dimeric assembly of the peptide was retained in membrane-mimicking systems containing negatively charged lipids and detergents. Arenicin-induced conductance was dependent on the lipid composition of the membrane. Arenicin low-conductivity pores were detected in the phosphatidylethanolamine-containing lipid mixture, whereas the high-conductivity pores were observed in an exclusively anionic lipid system. The measured conductivity levels agreed with the model in which arenicin antimicrobial activity was mediated by the formation of toroidal pores assembled of two, three, or four beta-structural peptide dimers and lipid molecules. The structural transitions involved in arenicin membrane-disruptive action are discussed. | ||
| - | + | Molecular mechanism of action of beta-hairpin antimicrobial peptide arenicin: oligomeric structure in dodecylphosphocholine micelles and pore formation in planar lipid bilayers.,Shenkarev ZO, Balandin SV, Trunov KI, Paramonov AS, Sukhanov SV, Barsukov LI, Arseniev AS, Ovchinnikova TV Biochemistry. 2011 Jul 19;50(28):6255-65. Epub 2011 Jun 24. PMID:21627330<ref>PMID:21627330</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2l8x" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arenicola marina]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arseniev AS]] | ||
| + | [[Category: Paramonov AS]] | ||
| + | [[Category: Shenkarev ZO]] | ||
| + | [[Category: Trunov KI]] | ||
Current revision
Spatial structure of antimicrobial peptide Arenicin-2 dimer in DPC micelles
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