2KJF
The solution structure of the circular bacteriocin carnocyclin A (CclA)
Summary for 2KJF
| Entry DOI | 10.2210/pdb2kjf/pdb |
| NMR Information | BMRB: 16319 |
| Descriptor | Carnocyclin-A (1 entity in total) |
| Functional Keywords | circular bacteriocin, antimicrobial peptide, helical, saposin-fold, antibiotic, antimicrobial, bacteriocin, antimicrobial protein |
| Biological source | Carnobacterium maltaromaticum (Carnobacterium piscicola) |
| Cellular location | Secreted: B2MVM5 |
| Total number of polymer chains | 1 |
| Total formula weight | 5885.01 |
| Authors | Martin-Visscher, L.A.,Gong, X.,Duszyk, M.,Vederas, J. (deposition date: 2009-05-28, release date: 2009-08-18, Last modification date: 2024-11-06) |
| Primary citation | Martin-Visscher, L.A.,Gong, X.,Duszyk, M.,Vederas, J.C. The three-dimensional structure of carnocyclin A reveals that many circular bacteriocins share a common structural motif. J.Biol.Chem., 284:28674-28681, 2009 Cited by PubMed Abstract: 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. PubMed: 19692336DOI: 10.1074/jbc.M109.036459 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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