2khf: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 2khf is ON HOLD  until Paper Publication
==Plantaricin J in DPC-micelles==
<StructureSection load='2khf' size='340' side='right'caption='[[2khf]]' scene=''>
== Structural highlights ==
<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='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=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>
== Function ==
[https://www.uniprot.org/uniprot/P71461_LACPN P71461_LACPN]
<div style="background-color:#fffaf0;">
== 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.


Authors: Rogne, P., Haugen, C., Kristiansen, P., Nissen-Meyer, J.
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<ref>PMID:19538999</ref>


Description: Plantaricin J in DPC-micelles
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 30 08:24:19 2009''
<div class="pdbe-citations 2khf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactiplantibacillus plantarum]]
[[Category: Large Structures]]
[[Category: Haugen C]]
[[Category: Kristiansen PE]]
[[Category: Nissen-Meyer J]]
[[Category: Rogne P]]
Retrieved from "https://proteopedia.org/2khf"