5UJQ

NMR Solution Structure of the Two-component Bacteriocin CbnXY

5UJQ の概要

• エントリーDOI: 10.2210/pdb5ujq/pdb
• NMR情報: BMRB: 30235
• 分子名称: Bacteriocin (1 entity in total)
• 機能のキーワード: antimicrobial protein
• 由来する生物種: Carnobacterium maltaromaticum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3098.69

構造登録者

Acedo, J.Z.,Towle, K.M.,Lohans, C.T.,McKay, R.T.,Miskolzie, M.,Doerksen, T.,Vederas, J.C.,Martin-Visscher, L.A. (登録日: 2017-01-18, 公開日: 2017-11-29, 最終更新日: 2024-05-15)

主引用文献

Acedo, J.Z.,Towle, K.M.,Lohans, C.T.,Miskolzie, M.,McKay, R.T.,Doerksen, T.A.,Vederas, J.C.,Martin-Visscher, L.A.
Identification and three-dimensional structure of carnobacteriocin XY, a class IIb bacteriocin produced by Carnobacteria.
FEBS Lett., 591:1349-1359, 2017

PubMed Abstract: 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 α-helix and a flexible C terminus. CbnY has two α-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.

PubMed: 28391617
DOI: 10.1002/1873-3468.12648

実験手法

SOLUTION NMR