2jpm: Difference between revisions
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<StructureSection load='2jpm' size='340' side='right' caption='[[2jpm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2jpm' size='340' side='right' caption='[[2jpm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jpm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2jpm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JPM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JPM FirstGlance]. <br> | ||
</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=2jpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jpm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jpm RCSB], [http://www.ebi.ac.uk/pdbsum/2jpm PDBsum]</span></td></tr> | </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=2jpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jpm OCA], [http://pdbe.org/2jpm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jpm RCSB], [http://www.ebi.ac.uk/pdbsum/2jpm PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ | [[http://www.uniprot.org/uniprot/LCGB_LACLL LCGB_LACLL]] Kills Lactococci. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2jpm" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacterium lactis lister 1873]] | ||
[[Category: Fimland, G]] | [[Category: Fimland, G]] | ||
[[Category: Kristiansen, P E]] | [[Category: Kristiansen, P E]] | ||
Revision as of 03:41, 11 September 2015
Lactococcin G-b in TFELactococcin G-b in TFE
Structural highlights
Function[LCGB_LACLL] Kills Lactococci. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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