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| | ==Structure of Glycocin F== | | ==Structure of Glycocin F== |
| - | <StructureSection load='2kuy' size='340' side='right' caption='[[2kuy]], [[NMR_Ensembles_of_Models | 12 NMR models]]' scene=''> | + | <StructureSection load='2kuy' size='340' side='right'caption='[[2kuy]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kuy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactobacillus_plantarum Lactobacillus plantarum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KUY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KUY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kuy]] 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=2KUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KUY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 12 models</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=2kuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kuy OCA], [http://pdbe.org/2kuy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kuy RCSB], [http://www.ebi.ac.uk/pdbsum/2kuy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kuy ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=2kuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kuy OCA], [https://pdbe.org/2kuy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kuy RCSB], [https://www.ebi.ac.uk/pdbsum/2kuy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kuy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GCCF_LACPN GCCF_LACPN]] Has antibacterial activity against L.plantarum ATCC 8014. In purified form, the activity is bacteriostatic (IC(50)=2 nM) rather than bactericidal.<ref>PMID:21251913</ref> | + | [https://www.uniprot.org/uniprot/GCCF_LACPN GCCF_LACPN] Has antibacterial activity against L.plantarum ATCC 8014. In purified form, the activity is bacteriostatic (IC(50)=2 nM) rather than bactericidal.<ref>PMID:21251913</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lactobacillus plantarum]] | + | [[Category: Lactiplantibacillus plantarum]] |
| - | [[Category: Claridge, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Edwards, P]] | + | [[Category: Claridge J]] |
| - | [[Category: Libich, D]] | + | [[Category: Edwards P]] |
| - | [[Category: Loo, T]] | + | [[Category: Libich D]] |
| - | [[Category: Norris, G]] | + | [[Category: Loo T]] |
| - | [[Category: Pascal, S]] | + | [[Category: Norris G]] |
| - | [[Category: Patchett, M]] | + | [[Category: Pascal S]] |
| - | [[Category: Schwalbe, M]] | + | [[Category: Patchett M]] |
| - | [[Category: Stepper, J]] | + | [[Category: Schwalbe M]] |
| - | [[Category: Venugopal, H]] | + | [[Category: Stepper J]] |
| - | [[Category: Antimicrobial protein]]
| + | [[Category: Venugopal H]] |
| - | [[Category: Bacteriocin]]
| + | |
| - | [[Category: Glycosylation]]
| + | |
| - | [[Category: Lactobacillus]]
| + | |
| - | [[Category: S-linked]]
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| Structural highlights
Function
GCCF_LACPN Has antibacterial activity against L.plantarum ATCC 8014. In purified form, the activity is bacteriostatic (IC(50)=2 nM) rather than bactericidal.[1]
Publication Abstract from PubMed
Bacteriocins are bacterial peptides with specific activity against competing species. They hold great potential as natural preservatives and for their probiotic effects. We show here nuclear magnetic resonance-based evidence that glycocin F, a 43-amino acid bacteriocin from Lactobacillus plantarum, contains two beta-linked N-acetylglucosamine moieties, attached via side chain linkages to a serine via oxygen, and to a cysteine via sulfur. The latter linkage is novel and has helped to establish a new type of post-translational modification, the S-linked sugar. The peptide conformation consists primarily of two alpha-helices held together by a pair of nested disulfide bonds. The serine-linked sugar is positioned on a short loop sequentially connecting the two helices, while the cysteine-linked sugar presents at the end of a long disordered C-terminal tail. The differing chemical and conformational stabilities of the two N-actetylglucosamine moieties provide clues about the possible mode of action of this bacteriostatic peptide.
Structural, dynamic, and chemical characterization of a novel s-glycosylated bacteriocin.,Venugopal H, Edwards PJ, Schwalbe M, Claridge JK, Libich DS, Stepper J, Loo T, Patchett ML, Norris GE, Pascal SM Biochemistry. 2011 Apr 12;50(14):2748-55. Epub 2011 Mar 21. PMID:21395300[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stepper J, Shastri S, Loo TS, Preston JC, Novak P, Man P, Moore CH, Havlicek V, Patchett ML, Norris GE. Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins. FEBS Lett. 2011 Feb 18;585(4):645-50. doi: 10.1016/j.febslet.2011.01.023. Epub, 2011 Jan 18. PMID:21251913 doi:http://dx.doi.org/10.1016/j.febslet.2011.01.023
- ↑ Venugopal H, Edwards PJ, Schwalbe M, Claridge JK, Libich DS, Stepper J, Loo T, Patchett ML, Norris GE, Pascal SM. Structural, dynamic, and chemical characterization of a novel s-glycosylated bacteriocin. Biochemistry. 2011 Apr 12;50(14):2748-55. Epub 2011 Mar 21. PMID:21395300 doi:10.1021/bi200217u
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