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Figure 5.
Figure 5. Features of the complex surface. Mutations of FtsY
interface residues that affect assembly of the complex, and
those that do not affect assembly but affect the subsequent
GTPase hydrolysis step,^15 are mapped onto the surface of FtsY
(gold, assembly defect; magenta, activity defect). The
orientation is looking into the GTPase binding site where bound
GTP is drawn as sticks. Activity defect mutations cluster (at
the bottom) near the FtsY active center, locating residues that
likely contribute to the activation region of the complex. The
relative position of the external nucleotide site is indicated
with an asterisk (*); however, formation of that binding site
requires assembly of the heterodimer. Figure 5. Features of
the complex surface. Mutations of FtsY interface residues that
affect assembly of the complex, and those that do not affect
assembly but affect the subsequent GTPase hydrolysis step,[3]^15
are mapped onto the surface of FtsY (gold, assembly defect;
magenta, activity defect). The orientation is looking into the
GTPase binding site where bound GTP is drawn as sticks. Activity
defect mutations cluster (at the bottom) near the FtsY active
center, locating residues that likely contribute to the
activation region of the complex. The relative position of the
external nucleotide site is indicated with an asterisk (*);
however, formation of that binding site requires assembly of the
heterodimer.
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