6go0: Difference between revisions
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==PLANTARICIN S-B IN 100 MM DPC MICELLES. THIS IS THE BETA PART OF THE BACTERIOCIN PLANTARICIN S== | |||
<StructureSection load='6go0' size='340' side='right' caption='[[6go0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6go0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GO0 FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6go0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6go0 OCA], [http://pdbe.org/6go0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6go0 RCSB], [http://www.ebi.ac.uk/pdbsum/6go0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6go0 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structure of the individual peptides of the two-peptide bacteriocin plantaricin S, an antimicrobial peptide produced by a Lactobacillus plantarum strain, has been determined in DPC micelles. The two peptides of plantaricin S, Pls-alpha and Pls-beta, form an alpha-helix from and including residue 8 to 24 with a less structured region around residue 16-19 and an amphiphilic alpha-helix from and including residue 7 to 23, respectively. Activity assays on single amino acid-substituted GxxxG and GxxxG-like motifs show that substituting the Ser and Gly residues in the G9xxxG13 motif in Pls-alpha and the S17xxxG21 motif in Pls-beta reduced or drastically reduced the antimicrobial activity. The two-peptide bacteriocin muricidin contains GxxxG-like motifs at similar positions and displays 40-50% amino acid identity with plantaricin S. Activity assays of combinations of the peptides that constitute the bacteriocins plantaricin S and muricidin show that some combinations are highly active. Furthermore, sequence alignments show that the motifs important for plantaricin S activity align with identical motifs in muricidin. Based on sequence comparison and activity assays, a membrane-inserted model of plantaricin S in which the two peptides are oriented antiparallel relative to each other and where the GxxxG and GxxxG-like motifs important for activity come close in space, is proposed. | |||
NMR structures and mutational analysis of the two peptides constituting the bacteriocin plantaricin S.,Ekblad B, Kristiansen PE Sci Rep. 2019 Feb 20;9(1):2333. doi: 10.1038/s41598-019-38518-6. PMID:30787405<ref>PMID:30787405</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6go0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ekblad, B]] | |||
[[Category: Kristiansen, P E]] | |||
[[Category: Antimicrobial protein]] | |||
[[Category: Antimicrobial protein bacteriocin menbrane interacting peptide]] | |||
Revision as of 07:28, 6 March 2019
PLANTARICIN S-B IN 100 MM DPC MICELLES. THIS IS THE BETA PART OF THE BACTERIOCIN PLANTARICIN S
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