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Hexamers of the type II secretion ATPase GspE from Vibrio cholerae with increased ATPase activity.


ABSTRACT: The type II secretion system (T2SS), a multiprotein machinery spanning two membranes in Gram-negative bacteria, is responsible for the secretion of folded proteins from the periplasm across the outer membrane. The critical multidomain T2SS assembly ATPase GspE(EpsE) had not been structurally characterized as a hexamer. Here, four hexamers of Vibrio cholerae GspE(EpsE) are obtained when fused to Hcp1 as an assistant hexamer, as shown with native mass spectrometry. The enzymatic activity of the GspE(EpsE)-Hcp1 fusions is ?20 times higher than that of a GspE(EpsE) monomer, indicating that increasing the local concentration of GspE(EpsE) by the fusion strategy was successful. Crystal structures of GspE(EpsE)-Hcp1 fusions with different linker lengths reveal regular and elongated hexamers of GspE(EpsE) with major differences in domain orientation within subunits, and in subunit assembly. SAXS studies on GspE(EpsE)-Hcp1 fusions suggest that even further variability in GspE(EpsE) hexamer architecture is likely.

SUBMITTER: Lu C 

PROVIDER: S-EPMC3775503 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature

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Hexamers of the type II secretion ATPase GspE from Vibrio cholerae with increased ATPase activity.

Lu Connie C   Turley Stewart S   Marionni Samuel T ST   Park Young-Jun YJ   Lee Kelly K KK   Patrick Marcella M   Shah Ripal R   Sandkvist Maria M   Bush Matthew F MF   Hol Wim G J WG  

Structure (London, England : 1993) 20130815 9


The type II secretion system (T2SS), a multiprotein machinery spanning two membranes in Gram-negative bacteria, is responsible for the secretion of folded proteins from the periplasm across the outer membrane. The critical multidomain T2SS assembly ATPase GspE(EpsE) had not been structurally characterized as a hexamer. Here, four hexamers of Vibrio cholerae GspE(EpsE) are obtained when fused to Hcp1 as an assistant hexamer, as shown with native mass spectrometry. The enzymatic activity of the Gs  ...[more]

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