5ujq
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NMR Solution Structure of the Two-component Bacteriocin CbnXY== | |
| + | <StructureSection load='5ujq' size='340' side='right'caption='[[5ujq]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ujq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Carnobacterium_maltaromaticum Carnobacterium maltaromaticum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UJQ FirstGlance]. <br> | ||
| + | </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=5ujq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ujq OCA], [https://pdbe.org/5ujq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ujq RCSB], [https://www.ebi.ac.uk/pdbsum/5ujq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ujq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q46312_CARML Q46312_CARML] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In this study, we report that CbnX (33 residues) and CbnY (29 residues) comprise a class IIb (two-component) bacteriocin in Carnobacteria. Individually, CbnX and CbnY are inactive, but together act synergistically to exert a narrow spectrum of activity. The structures of CbnX and CbnY in structure-inducing conditions were determined and strongly resemble other class IIb bacteriocins (i.e., LcnG, PlnEF, PlnJK). CbnX has an extended, amphipathic alpha-helix and a flexible C terminus. CbnY has two alpha-helices (one hydrophobic, one amphipathic) connected by a short loop and a cationic C terminus. CbnX and CbnY do not appear to interact directly and likely require a membrane-bound receptor to facilitate formation of the bacteriocin complex. This is the first class IIb bacteriocin reported for Carnobacteria. | ||
| - | + | Identification and three-dimensional structure of carnobacteriocin XY, a class IIb bacteriocin produced by Carnobacteria.,Acedo JZ, Towle KM, Lohans CT, Miskolzie M, McKay RT, Doerksen TA, Vederas JC, Martin-Visscher LA FEBS Lett. 2017 May;591(10):1349-1359. doi: 10.1002/1873-3468.12648. Epub 2017, Apr 27. PMID:28391617<ref>PMID:28391617</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5ujq" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Carnobacterium maltaromaticum]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Vederas | + | [[Category: Acedo JZ]] |
| + | [[Category: Doerksen T]] | ||
| + | [[Category: Lohans CT]] | ||
| + | [[Category: Martin-Visscher LA]] | ||
| + | [[Category: McKay RT]] | ||
| + | [[Category: Miskolzie M]] | ||
| + | [[Category: Towle KM]] | ||
| + | [[Category: Vederas JC]] | ||
Current revision
NMR Solution Structure of the Two-component Bacteriocin CbnXY
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