Abstract
The type VI secretion system (T6SS), commonly found in
Gram-negative bacteria, is responsible for exporting effector
proteins. The T6SS has been reported to be cytotoxic to host
cells. While the components and assembly of the T6SS complex
have been largely assessed, structural data on T6SS components
from virulent bacteria is remarkably insufficient.
Here, we report the crystal structure of Vibrio cholerae TssL
(VcTssL), a core component of T6SS. In spite of a relatively
low sequence identity, the overall structure of VcTssL is largely
similar to those from other bacterial homologs except
for several differences found in local structural elements. A
unique feature attributed to the C-terminal fragment of Vc-
TssL is a crystallographic artifact. This incidental feature of
VcTssL may provide insights into screening of molecular
partners for the cytoplasmic domain of TssL. Additionally,
our results may help in the design of molecular probes for a
detailed understanding of the functional relationship between
TssL and other T6SS components.
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