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Figure 9.
Fig. 9. Features of the binding pocket. (a) Overlay of the
binding pockets (residues 295–312) of two bound [wild-type
cAMP (red) and R307E (red)] and five [apo: R348A (gray) and
R307W (green)] structures. Glu298 and Met299, both highly
mobile, are highlighted. The side chains of Leu301 and position
307 (various mutants), as well as cAMP, are shown for reference.
(b) The positions of Leu301 and Phe327 in the bound (tan) and
apo (green) structures showing clear differences in the position
of the side chains between the two states, but not among the
structures in the individual states. (c) The position of the
Arg307 side chain is invariant regardless of state or mutation.
Side-chain position shown: R307 from cAMP-bound wild type (red),
R307 from the R348A apo structure (gray), Glu307 from the
R307E-bound structure (cyan), and two different Trp307 from the
R307W apo structure (green). (d) Stabilization of position 307
by interactions between its main chain and residues of a
parallel loop. Hydrogen bonds between the backbones at Arg307,
Gly266, and Glu267 from the cAMP-bound wild-type structure are
shown.
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