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| ==Solution structure of arenicin-1== | | ==Solution structure of arenicin-1== |
- | <StructureSection load='2jsb' size='340' side='right' caption='[[2jsb]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='2jsb' size='340' side='right'caption='[[2jsb]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2jsb]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JSB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JSB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jsb]] is a 1 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=2JSB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JSB FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jsb OCA], [http://pdbe.org/2jsb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jsb RCSB], [http://www.ebi.ac.uk/pdbsum/2jsb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jsb ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=2jsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jsb OCA], [https://pdbe.org/2jsb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jsb RCSB], [https://www.ebi.ac.uk/pdbsum/2jsb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jsb ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/ANN1_AREMA ANN1_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> | + | [https://www.uniprot.org/uniprot/ANN1_AREMA ANN1_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;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Fedders, H]] | |
- | [[Category: Gelhaus, C]] | |
- | [[Category: Groetzinger, J]] | |
- | [[Category: Hecht, O]] | |
- | [[Category: Jakovkin, I B]] | |
- | [[Category: Krasnosdembskaya, A D]] | |
- | [[Category: Leippe, M]] | |
- | [[Category: Antimicrobial]] | |
- | [[Category: Antimicrobial protein]] | |
- | [[Category: Arenicin]] | |
- | [[Category: Arenicin-1]] | |
| [[Category: Arenicola marina]] | | [[Category: Arenicola marina]] |
- | [[Category: Poreforming]] | + | [[Category: Large Structures]] |
| + | [[Category: Fedders H]] |
| + | [[Category: Gelhaus C]] |
| + | [[Category: Groetzinger J]] |
| + | [[Category: Hecht O]] |
| + | [[Category: Jakovkin IB]] |
| + | [[Category: Krasnosdembskaya AD]] |
| + | [[Category: Leippe M]] |
| Structural highlights
Function
ANN1_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.[1] [2]
Publication Abstract from PubMed
The solution structure and the mode of action of arenicin isoform 1, an antimicrobial peptide with a unique 18-residue loop structure, from the lugworm Arenicola marina were elucidated here. Arenicin folds into a two-stranded antiparallel beta-sheet. It exhibits high antibacterial activity at 37 and 4 degrees C against Gram-negative bacteria, including polymyxin B-resistant Proteus mirabilis. Bacterial killing occurs within minutes and is accompanied by membrane permeabilization, membrane detachment and release of cytoplasm. Interaction of arenicin with reconstituted membranes that mimic the lipopolysaccharide-containing outer membrane or the phospholipid-containing plasma membrane of Gram-negative bacteria exhibited no pronounced lipid specificity. Arenicin-induced current fluctuations in planar lipid bilayers correspond to the formation of short-lived heterogeneously structured lesions. Our results strongly suggest that membrane interaction plays a pivotal role in the antibacterial activity of arenicin.
Structure and mode of action of the antimicrobial peptide arenicin.,Andra J, Jakovkin I, Grotzinger J, Hecht O, Krasnosdembskaya AD, Goldmann T, Gutsmann T, Leippe M Biochem J. 2008 Feb 15;410(1):113-22. PMID:17935487[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ovchinnikova TV, Aleshina GM, Balandin SV, Krasnosdembskaya AD, Markelov ML, Frolova EI, Leonova YF, Tagaev AA, Krasnodembsky EG, Kokryakov VN. Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina. FEBS Lett. 2004 Nov 5;577(1-2):209-14. PMID:15527787 doi:http://dx.doi.org/10.1016/j.febslet.2004.10.012
- ↑ Andra J, Jakovkin I, Grotzinger J, Hecht O, Krasnosdembskaya AD, Goldmann T, Gutsmann T, Leippe M. Structure and mode of action of the antimicrobial peptide arenicin. Biochem J. 2008 Feb 15;410(1):113-22. PMID:17935487 doi:http://dx.doi.org/BJ20071051
- ↑ Andra J, Jakovkin I, Grotzinger J, Hecht O, Krasnosdembskaya AD, Goldmann T, Gutsmann T, Leippe M. Structure and mode of action of the antimicrobial peptide arenicin. Biochem J. 2008 Feb 15;410(1):113-22. PMID:17935487 doi:http://dx.doi.org/BJ20071051
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