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- | [[Image:2jsb.jpg|left|200px]]<br /><applet load="2jsb" size="350" color="white" frame="true" align="right" spinBox="true" | |
- | caption="2jsb" /> | |
- | '''Solution structure of arenicin-1'''<br /> | |
| | | |
- | ==Overview== | + | ==Solution structure of arenicin-1== |
- | 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. | + | <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 == |
| + | 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. |
| | | |
- | ==About this Structure==
| + | 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> |
- | 2JSB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JSB OCA].
| + | |
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- | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17935487 17935487]
| + | </div> |
- | [[Category: Single protein]] | + | <div class="pdbe-citations 2jsb" style="background-color:#fffaf0;"></div> |
- | [[Category: Fedders, H.]] | + | == References == |
- | [[Category: Gelhaus, C.]] | + | <references/> |
- | [[Category: Groetzinger, J.]] | + | __TOC__ |
- | [[Category: Hecht, O.]] | + | </StructureSection> |
- | [[Category: Jakovkin, I.B.]] | + | [[Category: Arenicola marina]] |
- | [[Category: Krasnosdembskaya, A.D.]] | + | [[Category: Large Structures]] |
- | [[Category: Leippe, M.]] | + | [[Category: Fedders H]] |
- | [[Category: antimicrobial]]
| + | [[Category: Gelhaus C]] |
- | [[Category: antimicrobial protein]]
| + | [[Category: Groetzinger J]] |
- | [[Category: arenicin]]
| + | [[Category: Hecht O]] |
- | [[Category: arenicin-1]]
| + | [[Category: Jakovkin IB]] |
- | [[Category: arenicola marina]]
| + | [[Category: Krasnosdembskaya AD]] |
- | [[Category: nmr]]
| + | [[Category: Leippe M]] |
- | [[Category: peptide]]
| + | |
- | [[Category: poreforming]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 17:22:35 2008''
| + | |
| 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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