2kjf
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The solution structure of the circular bacteriocin carnocyclin A (CclA)== |
| + | <StructureSection load='2kjf' size='340' side='right'caption='[[2kjf]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2kjf]] 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=2KJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KJF FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2kjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kjf OCA], [https://pdbe.org/2kjf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kjf RCSB], [https://www.ebi.ac.uk/pdbsum/2kjf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kjf ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CCLA_CARML CCLA_CARML] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Carnocyclin A (CclA) is a potent antimicrobial peptide from Carnobacterium maltaromaticum UAL307 that displays a broad spectrum of activity against numerous Gram-positive organisms. An amide bond links the N and C termini of this bacteriocin, imparting stability and structural integrity to this 60-amino acid peptide. CclA interacts with lipid bilayers in a voltage-dependent manner and forms anion selective pores. Several other circular bacteriocins have been reported, yet only one (enterocin AS-48) has been structurally characterized. We have now determined the solution structure of CclA by NMR and further examined its anion binding and membrane channel properties. The results reveal that CclA preferentially binds halide anions and has a structure that is surprisingly similar to that of AS-48 despite low sequence identity, different oligomeric state, and disparate function. CclA folds into a compact globular bundle, comprised of four helices surrounding a hydrophobic core. NMR studies show two fluoride ion binding modes for CclA. Our findings suggest that although other circular bacteriocins are likely to have diverse mechanisms of action, many may have a common structural motif. This shared three-dimensional arrangement resembles the fold of mammalian saposins, peptides that either directly lyse membranes or serve as activators of lipid-degrading enzymes. | ||
| - | + | The three-dimensional structure of carnocyclin A reveals that many circular bacteriocins share a common structural motif.,Martin-Visscher LA, Gong X, Duszyk M, Vederas JC J Biol Chem. 2009 Oct 16;284(42):28674-81. Epub 2009 Aug 18. PMID:19692336<ref>PMID:19692336</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2kjf" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Carnobacterium maltaromaticum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Duszyk M]] | ||
| + | [[Category: Gong X]] | ||
| + | [[Category: Martin-Visscher LA]] | ||
| + | [[Category: Vederas J]] | ||
Current revision
The solution structure of the circular bacteriocin carnocyclin A (CclA)
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