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PDBsum entry 4ksr
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Protein transport
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PDB id
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4ksr
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References listed in PDB file
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Key reference
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Title
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Hexamers of the type ii secretion atpase gspe from vibrio cholerae with increased atpase activity.
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Authors
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C.Lu,
S.Turley,
S.T.Marionni,
Y.J.Park,
K.K.Lee,
M.Patrick,
R.Shah,
M.Sandkvist,
M.F.Bush,
W.G.Hol.
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Ref.
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Structure, 2013,
21,
1707-1717.
[DOI no: ]
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PubMed id
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Abstract
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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.
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