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Figure 4.
Figure 4. Conformational Differences between ADP-Bound and
ATP-Bound MJ0796 MonomersThe crystal structure of Mg-ADP-bound
wild-type MJ0796 (Yuan et al., 2001) (lighter colors) is
superimposed on that of the Na-ATP-bound E171Q mutant (darker
colors) based on least-squares alignment of 65 Cα atoms
located in the α helix following the Walker A motif and the 6
β strands in the F1-type ATP binding core. The backbone and
sidechains of each model are color coded according to subdomain
organization as in Figure 2A. The crystal structure of the E171Q
mutant of MJ0796 bound to Mg-ADP is essentially identical to
that of the wild-type protein bound to the same ligand (data not
shown). This view shows the molecular surface of the monomer
facing the intersubunit interface in the nucleotide sandwich
dimer.
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