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[[Image:1ytr.png|left|200px]]


{{STRUCTURE_1ytr| PDB=1ytr |  SCENE= }}
==NMR structure of plantaricin a in dpc micelles, 20 structures==
<StructureSection load='1ytr' size='340' side='right'caption='[[1ytr]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ytr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactiplantibacillus_plantarum_WCFS1 Lactiplantibacillus plantarum WCFS1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YTR 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=1ytr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ytr OCA], [https://pdbe.org/1ytr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ytr RCSB], [https://www.ebi.ac.uk/pdbsum/1ytr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ytr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PLNA_LACPL PLNA_LACPL] This heat stable bacteriocin inhibits the growth of closely related Lactobacillus species. It may act as a pore-forming protein, creating a channel in the cell membrane through a "barrel stave" mechanism.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure in dodecyl phosphocholine micelles of the 26-mer membrane-permeabilizing bacteriocin-like pheromone plantaricin A (PlnA) has been determined by use of nuclear magnetic resonance spectroscopy. The peptide was unstructured in water but became partly structured upon exposure to micelles. An amphiphilic alpha-helix stretching from residue 12 to 21 (possibly also including residues 22 and 23) was then formed in the C-terminal part of the peptide, whereas the N-terminal part remained largely unstructured. PlnA exerted its membrane-permeabilizing antimicrobial activity through a nonchiral interaction with the target cell membrane because the d-enantiomeric form had the same activity as the natural l-form. This nonchiral interaction involved the amphiphilic alpha-helical region in the C-terminal half of PlnA because a 17-mer fragment that contains the amphiphilic alpha-helical part of the peptide had antimicrobial potency that was similar to that of the l- and d-enantiomeric forms of PlnA. Also the pheromone activity of PlnA depended on this nonchiral interaction because both the l- and d-enantiomeric forms of the 17-mer fragment inhibited the pheromone activity. The pheromone activity also involved, however, a chiral interaction between the N-terminal part of PlnA and its receptor because high concentrations of the l-form (but not the d-form) of a 5-mer fragment derived from the N-terminal part of PlnA had pheromone activity. The results thus reveal a novel mechanism whereby peptide pheromones such as PlnA may function. An initial nonchiral interaction with membrane lipids induces alpha-helical structuring in a segment of the peptide pheromone. The peptide becomes thereby sufficiently structured and properly positioned in the membrane interface, thus enabling it to engage in a chiral interaction with its receptor in or near the membrane water interface. This membrane-interacting mode of action explains why some peptide pheromones/hormones such as PlnA sometimes display antimicrobial activity in addition to their pheromone activity.


===NMR structure of plantaricin a in dpc micelles, 20 structures===
Structure and mode of action of the membrane-permeabilizing antimicrobial peptide pheromone plantaricin A.,Kristiansen PE, Fimland G, Mantzilas D, Nissen-Meyer J J Biol Chem. 2005 Jun 17;280(24):22945-50. Epub 2005 Apr 1. PMID:15805109<ref>PMID:15805109</ref>


{{ABSTRACT_PUBMED_15805109}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 1ytr" style="background-color:#fffaf0;"></div>
[[1ytr]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YTR OCA].
== References ==
[[Category: Fimland, G.]]
<references/>
[[Category: Kristiansen, P E.]]
__TOC__
[[Category: Mantzilas, D.]]
</StructureSection>
[[Category: Nissen-Meyer, J.]]
[[Category: Lactiplantibacillus plantarum WCFS1]]
[[Category: Amphipathic helix]]
[[Category: Large Structures]]
[[Category: Antibiotic]]
[[Category: Fimland G]]
[[Category: Micelle]]
[[Category: Kristiansen PE]]
[[Category: Pheromone]]
[[Category: Mantzilas D]]
[[Category: Nissen-Meyer J]]
Retrieved from "https://proteopedia.org/1ytr"