2M60

Enterocin 7B

2M60 の概要

• エントリーDOI: 10.2210/pdb2m60/pdb
• 関連するPDBエントリー: 2M5Z
• NMR情報: BMRB: 19101
• 分子名称: Enterocin JSB (1 entity in total)
• 機能のキーワード: leaderless bacteriocin, antimicrobial protein
• 由来する生物種: Enterococcus faecalis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5219.28

構造登録者

Lohans, C.T.,Towle, K.M.,Miskolzie, M.,McKay, R.T.,van Belkum, M.J.,McMullen, L.M.,Vederas, J.C. (登録日: 2013-03-18, 公開日: 2013-06-12, 最終更新日: 2024-10-30)

主引用文献

Lohans, C.T.,Towle, K.M.,Miskolzie, M.,McKay, R.T.,van Belkum, M.J.,McMullen, L.M.,Vederas, J.C.
Solution Structures of the Linear Leaderless Bacteriocins Enterocin 7A and 7B Resemble Carnocyclin A, a Circular Antimicrobial Peptide
Biochemistry, 52:3987-3994, 2013

PubMed Abstract: Leaderless bacteriocins are a class of ribosomally synthesized antimicrobial peptides that are produced by certain Gram-positive bacteria without an N-terminal leader section. These bacteriocins are of great interest due to their potent inhibition of many Gram-positive organisms, including food-borne pathogens such as Listeria and Clostridium spp. We now report the NMR solution structures of enterocins 7A and 7B, leaderless bacteriocins recently isolated from Enterococcus faecalis 710C. These are the first three-dimensional structures to be reported for bacteriocins of this class. Unlike most other linear Gram-positive bacteriocins, enterocins 7A and 7B are highly structured in aqueous conditions. Both peptides are primarily α-helical, adopting a similar overall fold. The structures can be divided into three separate α-helical regions: the N- and C-termini are both α-helical, separated by a central kinked α-helix. The overall structures bear an unexpected resemblance to carnocyclin A, a 60-residue peptide that is cyclized via an amide bond between the C- and N-termini and has a saposin fold. Because of synergism observed for other two-peptide leaderless bacteriocins, it was of interest to probe possible binding interactions between enterocins 7A and 7B. However, despite synergistic activity observed between these peptides, no significant binding interaction was observed based on NMR and isothermal calorimetry.

PubMed: 23725536
DOI: 10.1021/bi400359z

実験手法

SOLUTION NMR