Escherichia Coli GnsA is a regulator of phosphatidylethanolamine synthesis and
functions as a suppressor of both a secG null mutation and fabA6 mutations. GnsA
may also be a toxin with the cognate antitoxin YmcE. Here we report the crystal
structure of GnsA to 1.8 Å. GnsA forms a V shaped hairpin structure that is
tightly associated into a homodimer. Our comprehensive structural study suggests
that GnsA is structurally similar to an outer membrane protein, suggesting a
function of protein binding.