D
IPR049371

GspD-like, N0 domain

InterPro entry
Short nameGspD-like_N0
Overlapping
homologous
superfamilies
 

Description

GspD is a type II general secretion pathway protein involved in protein export. This entry represents the N0 domain found at the N-terminal of GspD type II secretins and its close homologues
[3, 2, 5, 1, 4]
. These proteins form a dodecameric ring, in which the N0 domain mediate extensive contacts suggesting that dodecameric N0 ring is an important feature of T2SS secretins
[1]
. This domain is also found in virion export proteins, proteins thought to form a channel across the host outer membrane for the purposes of extruding the bacteriophage.

References

1.A dodecameric ring-like structure of the N0 domain of the type II secretin from enterotoxigenic Escherichia coli. Korotkov KV, Delarosa JR, Hol WGJ. J Struct Biol 183, 354-362, (2013). PMID: 23820381

2.Structural and functional studies on the interaction of GspC and GspD in the type II secretion system. Korotkov KV, Johnson TL, Jobling MG, Pruneda J, Pardon E, Heroux A, Turley S, Steyaert J, Holmes RK, Sandkvist M, Hol WG. PLoS Pathog. 7, e1002228, (2011). View articlePMID: 21931548

3.Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Korotkov KV, Pardon E, Steyaert J, Hol WG. Structure 17, 255-65, (2009). View articlePMID: 19217396

4.Unraveling the Self-Assembly of the Pseudomonas aeruginosa XcpQ Secretin Periplasmic Domain Provides New Molecular Insights into Type II Secretion System Secreton Architecture and Dynamics. Douzi B, Trinh NTT, Michel-Souzy S, Desmyter A, Ball G, Barbier P, Kosta A, Durand E, Forest KT, Cambillau C, Roussel A, Voulhoux R. mBio 8, e01185-17, (2017). View articlePMID: 29042493

5.New insights into the assembly of bacterial secretins: structural studies of the periplasmic domain of XcpQ from Pseudomonas aeruginosa. Van der Meeren R, Wen Y, Van Gelder P, Tommassen J, Devreese B, Savvides SN. J Biol Chem 288, 1214-25, (2013). View articlePMID: 23188826

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