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Figure 5.
RelB induced conformation change in the active site of RelE.
A, active conformation of the E. coli RelE mRNA-binding site in
the absence of RelB antitoxin. The side chain of Arg^81 was
modeled based on the orientation of Ala^81 in the structure of
RelE^R81A/R83A. B, active site of RNase SA shows the catalytic
triad (Glu^54, Arg^69, and His^85) and the hydrophobic site
(Phe^37 and Tyr^86) for base packing. C, catalytic site of YoeB
in the YefM-free conformation shows the catalytic triad (Glu^46,
Arg^65, and His^83) and base anchor residues (Leu^48, Leu^52,
and Tyr^84). D, putative mRNA-binding site of E. coli RelE in
the presence of RelB[C] shows a large conformation disruption to
the active site. The side chain of Arg^81 is modeled based on
the orientation of Ala^81 in the structure of
RelE^R81A/R83A-RelB[C]. E, active site of archaeal aRelE in the
aRelB-aRelE complex shows an inactive conformation similar to
the RelE^R81A/R83A-RelB[C] complex. The C-terminal residues
(Tyr^89 and Lys^90) of aRelE are missing in the crystal
structure; they were arbitrarily rebuilt to estimate the
position of Tyr^89. F, catalytic active site of YoeB in the
YoeB-YefM complex shows the conformational change altered by
YefM binding.
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