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Figure 1.
Figure 1. An Npl3p-derived peptide binds Sky1p in a region
distal to the active site. (a) Domain maps of Sky1p and Npl3p.
Full-length Sky1p contains two kinase sub-domains (blue)
bifurcated by a spacer region (red). The Sky1p kinase domain is
also flanked by non-kinase core regions (white). A minimal
construct of Sky1p, Sky1pΔN(137)ΔS was used for
crystallization. Yellow rectangle denotes poly-histidine tag.
The RGG domain of Npl3p (red) contains eight RS dipeptide
repeats, the last of which is phosphorylated by Sky1p (denoted
by yellow-green). The serine at position 4 of the peptide
corresponds to the phosphorylated serine. (b) Surface rendition
of Sky1p/peptide/ADP complex. The peptide and ADP are shown in
yellow and SKy1p in blue. (c) 2F[o]−F[c] electron density map
(1σ) for both the Npl3p-derived peptide (left molecule) and ADP
(right molecule) binding. (d) An overlay of the small lobes
(residues 144−300) of the apo-kinase (blue) and the
peptide-bound kinase (red) shows that the kinase structure
remains mostly unchanged as a substrate peptide binds distal to
the active site.
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