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Figure 4.
Figure 4. Closed, Semi-Open, and Open Structures of MalK
Homodimer with Superimposed RDsThe distances between two H89
residues in a homodimer are indicated.(A) Superimposed closed
form with bound ATP (yellow) and semi-open form without bound
ATP (blue). The excellent overlap of the RDs is evident by the
green color resulting from the combination of yellow and blue
colors.(B) Overlay of the semi-open (blue) and the open (red)
nucleotide-free structures.
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