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Figure 2.
Figure 2. Sky1p and SRPK1 share a conserved substrate docking
groove. (a) Residues in Sky1p docking groove involved in the
interaction with the peptide/ADP composite substrate. Residues
labeled in cyan (I653, K657and W659) and red (K668) were mutated
to alanine in the Sky1p QM mutant. Green (D601, D617 and E624)
and red residues (K668) were mutated to alanine in the Sky1p 4M
mutant. Residues labeled in blue (L603, Y612, Q621 and V664)
make non-specific interactions with either the peptide or ADP.
Note that residues D617 and E624 form hydrogen bonds with the
adenine ring of ADP. (b) Interactions between SRPK1 docking
groove and a similar peptide as in (a) are shown. (c) The
sequence alignment of Sky1p and SRPK1 docking grooves shows that
the region is highly conserved between Sky1p and SRPK1.
Identical residues are shaded. (d) Kinetic analysis shows that
the docking groove of Sky1p is essential for substrate
phosphorylation.
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