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Figure 4.
Figure 4: Structural analysis of the GDPase reaction. a,
Superimposition of the active sites of hGBP1^LG  circle
GMP circle
AlF[4]^- (blue) and hGBP1^LG circle
GDP circle
AlF[3] (green) structures, respectively, showing the shift of
GMP for the second hydrolysis step. Black broken lines show
stabilizing polar interactions and red broken lines indicate
unfavourable vicinities between the nucleotide in the GDP circle
AlF[3] structure and the guanine cap residues as found in the
GMP
circle AlF[4]^- structure. b, Superimposition of
nucleotide-binding sites of hGBP1^LG circle
GMP (yellow, gold) and Ras circle
GDP (green; Protein Data Bank accession code 4Q21) structures
with the  -phosphate
of GMP occupying a similar position to that of the  -phosphate
of Ras circle
GDP. Arg 48 is pointing away from the active site. Red star
indicates possible steric hindrance between Lys 117 of the
(N/T)KxD motif from Ras and the GMP base conformation found in
hGBP1^LG.
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