|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Three-Dimensional Structure of the two Peptides that Constitute the Two-Peptide Bacteriocin Plantaracin EF== | | ==Three-Dimensional Structure of the two Peptides that Constitute the Two-Peptide Bacteriocin Plantaracin EF== |
| - | <StructureSection load='2jui' size='340' side='right' caption='[[2jui]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2jui' size='340' side='right'caption='[[2jui]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jui]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactobacillus_plantarum Lactobacillus plantarum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JUI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JUI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jui]] 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=2JUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JUI FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rlw|2rlw]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">plnE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1590 Lactobacillus plantarum])</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=2jui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jui OCA], [https://pdbe.org/2jui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jui RCSB], [https://www.ebi.ac.uk/pdbsum/2jui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jui ProSAT]</span></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=2jui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jui OCA], [http://pdbe.org/2jui PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jui RCSB], [http://www.ebi.ac.uk/pdbsum/2jui PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jui ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/P71470_LACPN P71470_LACPN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lactobacillus plantarum]] | + | [[Category: Lactiplantibacillus plantarum]] |
| - | [[Category: Fimland, G]] | + | [[Category: Large Structures]] |
| - | [[Category: Fimland, N]] | + | [[Category: Fimland G]] |
| - | [[Category: Kristiansen, P]] | + | [[Category: Fimland N]] |
| - | [[Category: Nissen-Meyer, J]] | + | [[Category: Kristiansen P]] |
| - | [[Category: Rogne, P]] | + | [[Category: Nissen-Meyer J]] |
| - | [[Category: Ampiphilic alpha helix]]
| + | [[Category: Rogne P]] |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
P71470_LACPN
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fimland N, Rogne P, Fimland G, Nissen-Meyer J, Kristiansen PE. Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin plantaricin EF. Biochim Biophys Acta. 2008 May 24;. PMID:18555030 doi:http://dx.doi.org/S1570-9639(08)00164-7
|
