View source for 2keh


==Plantaricin K in TFE==
<StructureSection load='2keh' size='340' side='right'caption='[[2keh]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2keh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactiplantibacillus_plantarum Lactiplantibacillus plantarum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KEH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2keh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2keh OCA], [https://pdbe.org/2keh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2keh RCSB], [https://www.ebi.ac.uk/pdbsum/2keh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2keh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/P71460_LACPN P71460_LACPN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structures of the two peptides, PlnJ and PlnK, that constitutes the two-peptide bacteriocin plantaricin JK have been solved in water/TFE and water/DPC-micellar solutions using nuclear magnetic resonance (NMR) spectroscopy. PlnJ, a 25 residue peptide, has an N-terminal amphiphilic alpha-helix between Trp-3 and Tyr-15. The 32 residues long PlnK forms a central amphiphilic alpha-helix between Gly-9 and Leu-24. Measurements of the effect on anti-microbial activity of single glycine replacements in PlnJ and PlnK show that Gly-13 and Gly-17 in both peptides are very sensitive, giving more than a 100-fold reduction in activity when large residues replace glycine. In variants where other glycine residues, Gly-20 in PlnJ and Gly-7, Gly-9, Gly-24 and Gly-25 in PlnK, were replaced, the activity was reduced less than 10-fold. It is proposed that the detrimental effect on activity when exchanging Gly-13 and Gly-17 in PlnJ and PlnK is a result of reduced ability of the two peptides to interact through the GxxxG-motifs constituting Gly-13 and Gly-17.

Three-dimensional structure of the two-peptide bacteriocin plantaricin JK.,Rogne P, Haugen C, Fimland G, Nissen-Meyer J, Kristiansen PE Peptides. 2009 Sep;30(9):1613-21. Epub 2009 Jun 16. PMID:19538999<ref>PMID:19538999</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2keh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Lactiplantibacillus plantarum]]
[[Category: Large Structures]]
[[Category: Haugen M]]
[[Category: Kristiansen P]]
[[Category: Nissen-Meyer J]]
[[Category: Rogne P]]