2jpm: Difference between revisions
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< | ==Lactococcin G-b in TFE== | ||
<StructureSection load='2jpm' size='340' side='right'caption='[[2jpm]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2jpm]] 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=2JPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JPM 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=2jpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jpm OCA], [https://pdbe.org/2jpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jpm RCSB], [https://www.ebi.ac.uk/pdbsum/2jpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jpm 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2jpm" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
[[Category: Lactococcus lactis]] | [[Category: Lactococcus lactis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Fimland | [[Category: Fimland G]] | ||
[[Category: Kristiansen | [[Category: Kristiansen PE]] | ||
[[Category: Nissen-Meyer | [[Category: Nissen-Meyer J]] | ||
[[Category: Rogne | [[Category: Rogne P]] | ||
Latest revision as of 19:38, 13 December 2023
Lactococcin G-b in TFELactococcin G-b in TFE
Structural highlights
FunctionLCGB_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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