5LFI

lactococcin A immunity protein

5LFI の概要

• エントリーDOI: 10.2210/pdb5lfi/pdb
• NMR情報: BMRB: 34018
• 分子名称: Lactococcin-A immunity protein (1 entity in total)
• 機能のキーワード: four-helix bundle, immunity protein, bacteriocin receptor, immune system
• 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: 13273.20

構造登録者

Persson, C.,Fuochi, V.,Pedersen, A.,Karlsson, B.G.,Nissen-Meyer, J.,Kristiansen, P.E.,Oppegard, C. (登録日: 2016-07-01, 公開日: 2016-11-16, 最終更新日: 2024-06-19)

主引用文献

Kristiansen, P.E.,Persson, C.,Fuochi, V.,Pedersen, A.,Karlsson, G.B.,Nissen-Meyer, J.,Oppegard, C.
Nuclear Magnetic Resonance Structure and Mutational Analysis of the Lactococcin A Immunity Protein.
Biochemistry, 55:6250-6257, 2016

PubMed Abstract: The class IId bacteriocin lactococcin A and the pediocin-like bacteriocins induce membrane leakage and cell death by specifically binding the mannose phophotransferase system (man-PTS) on their target cells. The bacteriocins' cognate immunity proteins that protect the producer cell from its own bacteriocin recognize and bind to the bacteriocin-man-PTS complex and thereby block membrane leakage. In this study, we have determined the three-dimensional structure of the lactococcin A immunity protein (LciA) by the use of nuclear magnetic resonance spectroscopy. LciA forms a four-helix bundle structure with a flexible C-terminal tail. Despite the low degree of sequence similarity between LciA and the pediocin-like immunity proteins, they share the same fold. However, there are certain differences between the structures. The C-terminal helix in LciA is considerably shorter than that observed in the pediocin-like immunity proteins, and the surface potentials of the immunity proteins differ. Truncated variants of LciA in which 6 or 10 of the C-terminal residues were removed yielded a reduced degree of protection, indicating that the unstructured C-terminal tail is important for the functionality of the immunity proteins.

PubMed: 27808503
DOI: 10.1021/acs.biochem.6b00848

実験手法

SOLUTION NMR