2LNV

Solution structure of GspC-HR of typeII secretion system

Summary for 2LNV

• Entry DOI: 10.2210/pdb2lnv/pdb
• NMR Information: BMRB: 18181
• Descriptor: General secretion pathway protein C (1 entity in total)
• Functional Keywords: transport protein
• Biological source: Dickeya dadantii
• Cellular location: Cell inner membrane (Probable): Q01564
• Total number of polymer chains: 1
• Total formula weight: 11138.30

Authors

Gu, S.,Kelly, G.,Pickersgill, R. (deposition date: 2012-01-05, release date: 2012-01-25, Last modification date: 2024-05-01)

Primary citation

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

Experimental method

SOLUTION NMR