2rlw
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2rlw is ON HOLD until Paper Publication Authors: Fimland, N., Rogne, P., Fimland, G., Nissen-Meyer, J., Kristiansen, P. Description: Three-Dimensio...) |
|||
| (10 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Three-Dimensional Structure of the two Peptides that Constitute the Two-Peptide Bacteriocin Plantaracin EF== | |
| + | <StructureSection load='2rlw' size='340' side='right'caption='[[2rlw]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2rlw]] 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=2RLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RLW 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=2rlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rlw OCA], [https://pdbe.org/2rlw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rlw RCSB], [https://www.ebi.ac.uk/pdbsum/2rlw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rlw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/P71469_LACPN P71469_LACPN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The three-dimensional structures of the two peptides plantaricin E (plnE; 33 residues) and plantaricin F (plnF; 34 residues) constituting the two-peptide bacteriocin plantaricin EF (plnEF) have been determined by nuclear magnetic resonance (NMR) spectroscopy in the presence of DPC micelles. PlnE has an N-terminal alpha-helix (residues 10-21), and a C-terminal alpha-helix-like structure (residues 25-31). PlnF has a long central alpha-helix (residues 7-32) with a kink of 38+/-7 degrees at Pro20. There is some flexibility in the helix in the kink region. Both helices in plnE are amphiphilic, while the helix in plnF is polar in its N-terminal half and amphiphilic in its C-terminal half. The alpha-helical content obtained by NMR spectroscopy is in agreement with CD studies. PlnE has two GxxxG motifs which are putative helix-helix interaction motifs, one at residues 5 to 9 and one at residues 20 to 24, while plnF has one such motif at residues 30 to 34. The peptides are flexible in these GxxxG regions. It is suggested that the two peptides lie parallel in a staggered fashion relative to each other and interact through helix-helix interactions involving the GxxxG motifs. | ||
| - | + | Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin plantaricin EF.,Fimland N, Rogne P, Fimland G, Nissen-Meyer J, Kristiansen PE Biochim Biophys Acta. 2008 May 24;. PMID:18555030<ref>PMID:18555030</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2rlw" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Lactiplantibacillus plantarum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fimland G]] | ||
| + | [[Category: Fimland N]] | ||
| + | [[Category: Kristiansen P]] | ||
| + | [[Category: Nissen-Meyer J]] | ||
| + | [[Category: Rogne P]] | ||
Current revision
Three-Dimensional Structure of the two Peptides that Constitute the Two-Peptide Bacteriocin Plantaracin EF
| |||||||||||
