2MLU

Structure of the antimicrobial peptide LsbB in DPC micelles

2MLU の概要

• エントリーDOI: 10.2210/pdb2mlu/pdb
• 関連するPDBエントリー: 2MLV
• NMR情報: BMRB: 19832
• 分子名称: LsbB (1 entity in total)
• 機能のキーワード: bacteriocin, antimicrobial peptide, receptor binding domain, mode of killing, dpc, antimicrobial protein
• 由来する生物種: Lactococcus lactis subsp. lactis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3418.02

構造登録者

Kristiansen, P.,Ovchinnikov, K.,Diep, D. (登録日: 2014-03-05, 公開日: 2014-07-16, 最終更新日: 2024-05-15)

主引用文献

Ovchinnikov, K.V.,Kristiansen, P.E.,Uzelac, G.,Topisirovic, L.,Kojic, M.,Nissen-Meyer, J.,Nes, I.F.,Diep, D.B.
Defining the Structure and Receptor Binding Domain of the Leaderless Bacteriocin LsbB.
J.Biol.Chem., 289:23838-23845, 2014

PubMed Abstract: LsbB is a class II leaderless lactococcal bacteriocin of 30 amino acids. In the present work, the structure and function relationship of LsbB was assessed. Structure determination by NMR spectroscopy showed that LsbB has an N-terminal α-helix, whereas the C-terminal of the molecule remains unstructured. To define the receptor binding domain of LsbB, a competition assay was performed in which a systematic collection of truncated peptides of various lengths covering different parts of LsbB was used to inhibit the antimicrobial activity of LsbB. The results indicate that the outmost eight-amino acid sequence at the C-terminal end is likely to contain the receptor binding domain because only truncated fragments from this region could antagonize the antimicrobial activity of LsbB. Furthermore, alanine substitution revealed that the tryptophan in position 25 (Trp(25)) is crucial for the blocking activity of the truncated peptides, as well as for the antimicrobial activity of the full-length bacteriocin. LsbB shares significant sequence homology with five other leaderless bacteriocins, especially at their C-terminal halves where all contain a conserved KXXXGXXPWE motif, suggesting that they might recognize the same receptor as LsbB. This notion was supported by the fact that truncated peptides with sequences derived from the C-terminal regions of two LsbB-related bacteriocins inhibited the activity of LsbB, in the same manner as found with the truncated version of LsbB. Taken together, these structure-function studies provide strong evidence that the receptor-binding parts of LsbB and sequence-related bacteriocins are located in their C-terminal halves.

PubMed: 24993828
DOI: 10.1074/jbc.M114.579698

実験手法

SOLUTION NMR