Structural similarity of secretins from type II and type III secretion systems. - Archive ouverte HAL
Article Dans Une Revue Structure Année : 2014

Structural similarity of secretins from type II and type III secretion systems.

Résumé

Secretins, the outer membrane components of several secretion systems in Gram-negative bacteria, assemble into channels that allow exoproteins to traverse the membrane. The membrane-inserted, multimeric regions of PscC, the Pseudomonas aeruginosa type III secretion system secretin, and PulD, the Klebsiella oxytoca type II secretion system secretin, were purified after cell-free synthesis and their structures analyzed by single particle cryoelectron microscopy. Both homomultimeric, barrel-like structures display a "cup and saucer" architecture. The "saucer" region of both secretins is composed of two distinct rings, with that of PulD being less segmented than that of PscC. Both secretins have a central chamber that is occluded by a plug linked to the chamber walls through hairpin-like structures. Comparisons with published structures from other bacterial systems reveal that secretins have regions of local structural flexibility, probably reflecting their evolved functions in protein secretion and needle assembly.

Dates et versions

hal-01100291 , version 1 (06-01-2015)

Identifiants

Citer

Tommaso Tosi, Leandro F Estrozi, Viviana Job, Ingrid Guilvout, Anthony P Pugsley, et al.. Structural similarity of secretins from type II and type III secretion systems.. Structure, 2014, 22 (9), pp.1348-1355. ⟨10.1016/j.str.2014.07.005⟩. ⟨hal-01100291⟩
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