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| | ==Plantaricin J in DPC-micelles== | | ==Plantaricin J in DPC-micelles== |
| - | <StructureSection load='2khf' size='340' side='right'caption='[[2khf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2khf' size='340' side='right'caption='[[2khf]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2khf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"lactobacillus_arabinosus"_fred_et_al. "lactobacillus arabinosus" fred et al.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KHF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KHF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2khf]] 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=2KHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KHF FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">plnJ, lp_0406 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1590 "Lactobacillus arabinosus" Fred et al.])</td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2khf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2khf OCA], [http://pdbe.org/2khf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2khf RCSB], [http://www.ebi.ac.uk/pdbsum/2khf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2khf ProSAT]</span></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=2khf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2khf OCA], [https://pdbe.org/2khf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2khf RCSB], [https://www.ebi.ac.uk/pdbsum/2khf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2khf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/P71461_LACPN P71461_LACPN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lactobacillus arabinosus fred et al]] | + | [[Category: Lactiplantibacillus plantarum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Haugen, C]] | + | [[Category: Haugen C]] |
| - | [[Category: Kristiansen, P E]] | + | [[Category: Kristiansen PE]] |
| - | [[Category: Nissen-Meyer, J]] | + | [[Category: Nissen-Meyer J]] |
| - | [[Category: Rogne, P]] | + | [[Category: Rogne P]] |
| - | [[Category: Anti-microbial]]
| + | |
| - | [[Category: Antimicrobial protein]]
| + | |
| - | [[Category: Bacteriocin]]
| + | |
| - | [[Category: Two-peptide]]
| + | |
| Structural highlights
Function
P71461_LACPN
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rogne P, Haugen C, Fimland G, Nissen-Meyer J, Kristiansen PE. Three-dimensional structure of the two-peptide bacteriocin plantaricin JK. Peptides. 2009 Sep;30(9):1613-21. Epub 2009 Jun 16. PMID:19538999 doi:10.1016/j.peptides.2009.06.010
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