2jsb
From Proteopedia
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| - | [[Image:2jsb.jpg|left|200px]] | ||
| - | + | ==Solution structure of arenicin-1== | |
| - | + | <StructureSection load='2jsb' size='340' side='right'caption='[[2jsb]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <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='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> | |
| - | + | == Function == | |
| - | + | [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;"> | |
| - | + | == Publication Abstract from PubMed == | |
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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. | 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<ref>PMID:17935487</ref> | |
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| - | 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 | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2jsb" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arenicola marina]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fedders H]] | ||
| + | [[Category: Gelhaus C]] | ||
| + | [[Category: Groetzinger J]] | ||
| + | [[Category: Hecht O]] | ||
| + | [[Category: Jakovkin IB]] | ||
| + | [[Category: Krasnosdembskaya AD]] | ||
| + | [[Category: Leippe M]] | ||
Current revision
Solution structure of arenicin-1
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