2mij
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NMR structure of the S-linked glycopeptide sublancin 168== | |
| + | <StructureSection load='2mij' size='340' side='right'caption='[[2mij]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mij]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MIJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 models</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</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=2mij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mij OCA], [https://pdbe.org/2mij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mij RCSB], [https://www.ebi.ac.uk/pdbsum/2mij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mij ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SUNA_BACSU SUNA_BACSU] Bacteriocin active against Gram-positive bacteria. Inhibits B.cereus spore outgrowth, after the germination stage, approximately 1000-fold better than it inhibits exponential growth of the same cells. Inhibits B.subtilis strain ATCC 6633.<ref>PMID:21196935</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sublancin 168 is a member of a small group of glycosylated antimicrobial peptides known as glycocins. The solution structure of sublancin 168, a 37-amino-acid peptide produced by Bacillus subtilis 168, has been solved by nuclear magnetic resonance (NMR) spectroscopy. Sublancin comprises two alpha-helices and a well-defined interhelical loop. The two helices span residues 6-16 and 26-35, and the loop region encompasses residues 17-25. The 9-amino-acid loop region contains a beta-S-linked glucose moiety attached to Cys22. Hydrophobic interactions as well as hydrogen bonding are responsible for the well-structured loop region. The three-dimensional structure provides an explanation for the previously reported extraordinary high stability of sublancin 168. | ||
| - | + | NMR Structure of the S-Linked Glycopeptide Sublancin 168.,Garcia De Gonzalo CV, Zhu L, Oman TJ, van der Donk WA ACS Chem Biol. 2014 Jan 17. PMID:24405370<ref>PMID:24405370</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2mij" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus subtilis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Garcia De Gonzalo CV]] | ||
| + | [[Category: Oman TJ]] | ||
| + | [[Category: Zhu L]] | ||
| + | [[Category: Van der Donk WA]] | ||
Current revision
NMR structure of the S-linked glycopeptide sublancin 168
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