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Figure 5.
Figure 5. The Relay Controls the Position of the Converter to
which It Is Linked by Strong Conserved InteractionsRibbon
diagram of the interface between the relay (yellow) and the
converter (β sheet and last helix in green) in chicken S1 (A),
scallop S1 complexed with MgADP (B), and smooth MDE–AlF[4]^−
(C) oriented so that the converters superimpose. Note that the
orientation of the last three turns of the HP helix (yellow) is
similar in all these structures, since three glutamate residues
of this helix (brown) interact with residues of the converter
(cyan) in all three states. In contrast, the conformation of the
loop of the relay (yellow) is very different and is most rigid
in (C) where it interacts with the SH1 helix (red).
Conformational changes at both ends of the relay allow the
orientation of the lower 50 kDa subdomain (white, HP and HQ
helices) to differ with respect to that of the converter in
these three states. Note also how the environment around the
tryptophane residue (blue) of the relay varies in the three
states.
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