5EDJ

Crystal structure of the Neisseria meningitidis iron-regulated outer membrane lipoprotein FrpD

5EDJ の概要

• エントリーDOI: 10.2210/pdb5edj/pdb
• 関連するPDBエントリー: 5EDF
• 分子名称: FrpC operon protein (2 entities in total)
• 機能のキーワード: iron-regulated protein frpd, frpc-binding protein, novel fold, membrane protein, unknown function
• 由来する生物種: Neisseria meningitidis MC58
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27027.99

構造登録者

Sviridova, E.,Bumba, L.,Rezacova, P.,Sebo, P.,Kuta Smatanova, I. (登録日: 2015-10-21, 公開日: 2017-02-01, 最終更新日: 2024-11-20)

主引用文献

Sviridova, E.,Rezacova, P.,Bondar, A.,Veverka, V.,Novak, P.,Schenk, G.,Svergun, D.I.,Kuta Smatanova, I.,Bumba, L.
Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis.
Sci Rep, 7:40408-40408, 2017

PubMed Abstract: The iron-regulated protein FrpD from Neisseria meningitidis is an outer membrane lipoprotein that interacts with very high affinity (K ~ 0.2 nM) with the N-terminal domain of FrpC, a Type I-secreted protein from the Repeat in ToXin (RTX) protein family. In the presence of Ca, FrpC undergoes Ca -dependent protein trans-splicing that includes an autocatalytic cleavage of the Asp-Pro peptide bond and formation of an Asp-Lys isopeptide bond. Here, we report the high-resolution structure of FrpD and describe the structure-function relationships underlying the interaction between FrpD and FrpC. We identified FrpD residues involved in FrpC binding, which enabled localization of FrpD within the low-resolution SAXS model of the FrpD-FrpC complex. Moreover, the trans-splicing activity of FrpC resulted in covalent linkage of the FrpC fragment to plasma membrane proteins of epithelial cells in vitro, suggesting that formation of the FrpD-FrpC complex may be involved in the interaction of meningococci with the host cell surface.

PubMed: 28084396
DOI: 10.1038/srep40408

実験手法

X-RAY DIFFRACTION (2.3 Å)