2N2E

NMR solution structure of the C-terminal domain of NisI, a lipoprotein from Lactococcus lactis which confers immunity against nisin

2N2E の概要

• エントリーDOI: 10.2210/pdb2n2e/pdb
• NMR情報: BMRB: 25194
• 分子名称: Nisin immunity protein (1 entity in total)
• 機能のキーワード: lantibiotic self-immunity protein, antibiotic, lantibiotic-binding protein
• 由来する生物種: Lactococcus lactis subsp. lactis (firmicutes)
• 細胞内の位置: Cell membrane ; Lipid-anchor : P42708
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14493.79

構造登録者

Hacker, C.,Christ, N.A.,Korn, S.,Duchardt-Ferner, E.,Hellmich, U.A.,Duesterhus, S.,Koetter, P.,Entian, K.,Woehnert, J. (登録日: 2015-05-08, 公開日: 2015-10-21, 最終更新日: 2024-05-15)

主引用文献

Hacker, C.,Christ, N.A.,Duchardt-Ferner, E.,Korn, S.,Gobl, C.,Berninger, L.,Dusterhus, S.,Hellmich, U.A.,Madl, T.,Kotter, P.,Entian, K.D.,Wohnert, J.
The Solution Structure of the Lantibiotic Immunity Protein NisI and Its Interactions with Nisin.
J.Biol.Chem., 290:28869-28886, 2015

PubMed Abstract: Many Gram-positive bacteria produce lantibiotics, genetically encoded and posttranslationally modified peptide antibiotics, which inhibit the growth of other Gram-positive bacteria. To protect themselves against their own lantibiotics these bacteria express a variety of immunity proteins including the LanI lipoproteins. The structural and mechanistic basis for LanI-mediated lantibiotic immunity is not yet understood. Lactococcus lactis produces the lantibiotic nisin, which is widely used as a food preservative. Its LanI protein NisI provides immunity against nisin but not against structurally very similar lantibiotics from other species such as subtilin from Bacillus subtilis. To understand the structural basis for LanI-mediated immunity and their specificity we investigated the structure of NisI. We found that NisI is a two-domain protein. Surprisingly, each of the two NisI domains has the same structure as the LanI protein from B. subtilis, SpaI, despite the lack of significant sequence homology. The two NisI domains and SpaI differ strongly in their surface properties and function. Additionally, SpaI-mediated lantibiotic immunity depends on the presence of a basic unstructured N-terminal region that tethers SpaI to the membrane. Such a region is absent from NisI. Instead, the N-terminal domain of NisI interacts with membranes but not with nisin. In contrast, the C-terminal domain specifically binds nisin and modulates the membrane affinity of the N-terminal domain. Thus, our results reveal an unexpected structural relationship between NisI and SpaI and shed light on the structural basis for LanI mediated lantibiotic immunity.

PubMed: 26459561
DOI: 10.1074/jbc.M115.679969

実験手法

SOLUTION NMR