View source for 2jpk


==Lactococcin G-b in DPC==
<StructureSection load='2jpk' size='340' side='right'caption='[[2jpk]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jpk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JPK 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=2jpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jpk OCA], [https://pdbe.org/2jpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jpk RCSB], [https://www.ebi.ac.uk/pdbsum/2jpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jpk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LCGB_LACLL LCGB_LACLL] Kills Lactococci.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structures of the two peptides, lactococcin G-alpha (LcnG-alpha; contains 39 residues) and lactococcin G-beta (LcnG-beta, contains 35 residues), that constitute the two-peptide bacteriocin lactococcin G (LcnG) have been determined by nuclear magnetic resonance (NMR) spectroscopy in the presence of DPC micelles and TFE. In DPC, LcnG-alpha has an N-terminal alpha-helix (residues 3-21) that contains a GxxxG helix-helix interaction motif (residues 7-11) and a less well defined C-terminal alpha-helix (residues 24-34), and in between (residues 18-22) there is a second somewhat flexible GxxxG-motif. Its structure in TFE was similar. In DPC, LcnG-beta has an N-terminal alpha-helix (residues 6-19). The region from residues 20 to 35, which also contains a flexible GxxxG-motif (residues 18-22), appeared to be fairly unstructured in DPC. In the presence of TFE, however, the region between and including residues 23 and 32 formed a well defined alpha-helix. The N-terminal helix between and including residues 6 and 19 seen in the presence of DPC, was broken at residues 8 and 9 in the presence of TFE. The N-terminal helices, both in LcnG-alpha and -beta, are amphiphilic. We postulate that LcnG-alpha and -beta have a parallel orientation and interact through helix-helix interactions involving the first GxxxG (residues 7-11) motif in LcnG-alpha and the one (residues 18-22) in LcnG-beta, and that they thus lie in a staggered fashion relative to each other.

Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin lactococcin G.,Rogne P, Fimland G, Nissen-Meyer J, Kristiansen PE Biochim Biophys Acta. 2007 Dec 15;. PMID:18187052<ref>PMID:18187052</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2jpk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactococcus lactis]]
[[Category: Large Structures]]
[[Category: Fimland G]]
[[Category: Kristiansen PE]]
[[Category: Nissen-Meyer J]]
[[Category: Rogne P]]