2LNV

Solution structure of GspC-HR of typeII secretion system

2LNV の概要

• エントリーDOI: 10.2210/pdb2lnv/pdb
• NMR情報: BMRB: 18181
• 分子名称: General secretion pathway protein C (1 entity in total)
• 機能のキーワード: transport protein
• 由来する生物種: Dickeya dadantii
• 細胞内の位置: Cell inner membrane (Probable): Q01564
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11138.30

構造登録者

Gu, S.,Kelly, G.,Pickersgill, R. (登録日: 2012-01-05, 公開日: 2012-01-25, 最終更新日: 2024-05-01)

主引用文献

Gu, S.,Kelly, G.,Wang, X.,Frenkiel, T.,Shevchik, V.E.,Pickersgill, R.W.
Solution Structure of Homology Region (HR) Domain of Type II Secretion System.
J.Biol.Chem., 287:9072-9080, 2012

PubMed Abstract: The type II secretion system of Gram-negative bacteria is important for bacterial pathogenesis and survival; it is composed of 12 mostly multimeric core proteins, which build a sophisticated secretion machine spanning both bacterial membranes. OutC is the core component of the inner membrane subcomplex thought to be involved in both recognition of substrate and interaction with the outer membrane secretin OutD. Here, we report the solution structure of the HR domain of OutC and explore its interaction with the secretin. The HR domain adopts a β-sandwich-like fold consisting of two β-sheets each composed of three anti-parallel β-strands. This structure is strikingly similar to the periplasmic region of PilP, an inner membrane lipoprotein from the type IV pilus system highlighting the common evolutionary origin of these two systems and showing that all the core components of the type II secretion system have a structural or sequence ortholog within the type IV pili system. The HR domain is shown to interact with the N0 domain of the secretin. The importance of this interaction is explored in the context of the functional secretion system.

PubMed: 22253442
DOI: 10.1074/jbc.M111.300624

実験手法

SOLUTION NMR