3OSS

The crystal structure of enterotoxigenic Escherichia coli GspC-GspD complex from the type II secretion system

3OSS の概要

• エントリーDOI: 10.2210/pdb3oss/pdb
• 分子名称: TYPE 2 SECRETION SYSTEM, GSPC, TYPE 2 SECRETION SYSTEM, SECRETIN GSPD, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: general secretory pathway, hr domain, secretin, lanthanide-binding tag, protein transport
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell outer membrane : E3PJ86
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27387.62

構造登録者

Korotkov, K.V.,Pruneda, J.,Hol, W.G.J. (登録日: 2010-09-09, 公開日: 2011-08-03, 最終更新日: 2023-09-06)

主引用文献

Korotkov, K.V.,Johnson, T.L.,Jobling, M.G.,Pruneda, J.,Pardon, E.,Heroux, A.,Turley, S.,Steyaert, J.,Holmes, R.K.,Sandkvist, M.,Hol, W.G.
Structural and functional studies on the interaction of GspC and GspD in the type II secretion system.
Plos Pathog., 7:e1002228-e1002228, 2011

PubMed Abstract: Type II secretion systems (T2SSs) are critical for secretion of many proteins from Gram-negative bacteria. In the T2SS, the outer membrane secretin GspD forms a multimeric pore for translocation of secreted proteins. GspD and the inner membrane protein GspC interact with each other via periplasmic domains. Three different crystal structures of the homology region domain of GspC (GspC(HR)) in complex with either two or three domains of the N-terminal region of GspD from enterotoxigenic Escherichia coli show that GspC(HR) adopts an all-β topology. N-terminal β-strands of GspC and the N0 domain of GspD are major components of the interface between these inner and outer membrane proteins from the T2SS. The biological relevance of the observed GspC-GspD interface is shown by analysis of variant proteins in two-hybrid studies and by the effect of mutations in homologous genes on extracellular secretion and subcellular distribution of GspC in Vibrio cholerae. Substitutions of interface residues of GspD have a dramatic effect on the focal distribution of GspC in V. cholerae. These studies indicate that the GspC(HR)-GspD(N0) interactions observed in the crystal structure are essential for T2SS function. Possible implications of our structures for the stoichiometry of the T2SS and exoprotein secretion are discussed.

PubMed: 21931548
DOI: 10.1371/journal.ppat.1002228

実験手法

X-RAY DIFFRACTION (2.63 Å)