2KJF

The solution structure of the circular bacteriocin carnocyclin A (CclA)

2KJF の概要

• エントリーDOI: 10.2210/pdb2kjf/pdb
• NMR情報: BMRB: 16319
• 分子名称: Carnocyclin-A (1 entity in total)
• 機能のキーワード: circular bacteriocin, antimicrobial peptide, helical, saposin-fold, antibiotic, antimicrobial, bacteriocin, antimicrobial protein
• 由来する生物種: Carnobacterium maltaromaticum (Carnobacterium piscicola)
• 細胞内の位置: Secreted: B2MVM5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5885.01

構造登録者

Martin-Visscher, L.A.,Gong, X.,Duszyk, M.,Vederas, J. (登録日: 2009-05-28, 公開日: 2009-08-18, 最終更新日: 2024-11-06)

主引用文献

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

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: 19692336
DOI: 10.1074/jbc.M109.036459

実験手法

SOLUTION NMR