2jpk: Difference between revisions
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==Lactococcin G-b in DPC== | ==Lactococcin G-b in DPC== | ||
<StructureSection load='2jpk' size='340' side='right' caption='[[2jpk]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2jpk' size='340' side='right'caption='[[2jpk]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jpk]] 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=2JPK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JPK FirstGlance]. <br> | <table><tr><td colspan='2'>[[2jpk]] 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=2JPK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JPK FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacterium lactis lister 1873]] | [[Category: Bacterium lactis lister 1873]] | ||
[[Category: Large Structures]] | |||
[[Category: Fimland, G]] | [[Category: Fimland, G]] | ||
[[Category: Kristiansen, P E]] | [[Category: Kristiansen, P E]] | ||
Revision as of 09:47, 19 February 2020
Lactococcin G-b in DPCLactococcin G-b in DPC
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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