View source for 2jni


==Spatial structure of antimicrobial peptide arenicin-2 in aqueous solution==
<StructureSection load='2jni' size='340' side='right'caption='[[2jni]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jni]] 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=2JNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JNI 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=2jni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jni OCA], [https://pdbe.org/2jni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jni RCSB], [https://www.ebi.ac.uk/pdbsum/2jni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jni 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 ==
Arenicins are 21-residue cationic antimicrobial peptides, isolated from marine polychaeta Arenicola marina. In order to determine a high-resolution three-dimensional structure of arenicin-2, the recombinant peptide was overexpressed as a fused form in Escherichia coli. Both arenicin isoforms were synthesized using the Fmoc-based solid-phase strategy. Recombinant and synthetic arenicins were purified, and their antimicrobial and spectroscopic properties were analyzed. NMR investigation shows that in water solution arenicin-2 displays a prolonged beta-hairpin, formed by two antiparallel beta-strands and stabilized by one disulfide and nine hydrogen bonds. A significant right-handed twist in the beta-sheet is deprived the peptide surface of amphipathicity. CD spectroscopic analysis indicates that arenicin-2 binds to the SDS and DPC micelles, and conformation of the peptide is significantly changed upon binding. Arenicin strongly binds to anionic lipid (POPE/POPG) vesicles in contrast with zwitterionic (POPC) ones. These results suggest that arenicins are membrane active peptides and point to possible mechanism of their selectivity toward bacterial cells.

Recombinant expression, synthesis, purification, and solution structure of arenicin.,Ovchinnikova TV, Shenkarev ZO, Nadezhdin KD, Balandin SV, Zhmak MN, Kudelina IA, Finkina EI, Kokryakov VN, Arseniev AS Biochem Biophys Res Commun. 2007 Aug 17;360(1):156-62. Epub 2007 Jun 14. PMID:17585874<ref>PMID:17585874</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2jni" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arenicola marina]]
[[Category: Large Structures]]
[[Category: Arseniev AS]]
[[Category: Balandin SV]]
[[Category: Finkina EI]]
[[Category: Kokryakov VN]]
[[Category: Kudelina IA]]
[[Category: Nadezhdin KD]]
[[Category: Ovchinnikova TV]]
[[Category: Shenkarev ZO]]
[[Category: Zhmak MN]]