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Figure 1.
Fig. 1. Overall structure of the adenylate binding region from
S. pombe AMPK with bound AMP. The ATP-bound form is nearly
identical (fig. S6) and reveals no global structural changes
attributable to nucleotide identity. (A) Ribbon diagram of a
single heterotrimer, with  , ß, and
 subunits colored
yellow, blue, and green, respectively. The single molecule of
bound AMP is shown in CPK representation, and connections to the
GBD and KD at the N-termini of the ß and subunits,
respectively, are indicated. (B) View rotated 90°,
highlighting the adenylate binding entrance (AXP) and phosphate
binding tunnel, which is capped on the putative KD-interaction
surface by a polar flap from the ß subunit. The structure
corresponds to a heterotrimer defined by limited proteolysis, as
indicated in (C): hatched regions were excluded. Each of the two
crystal forms reported here includes a dimer of trimers in the
asymmetric unit (D). Analytical ultracentrifugation analysis
also demonstrates a dimer of trimers configuration.
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