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. 2016 Aug 4;35(19):2139–2151. doi: 10.15252/embj.201694082

Figure 2. Structure and nucleotide/inhibitor binding by budding yeast Hrr25.

Figure 2

  1. Domain diagram of crystallized Hrr25 constructs from Saccharomyces cerevisiae and Candida glabrata, missing the P/Q‐rich C‐terminal domain.
  2. Structures of S. cerevisiae Hrr251–394 K38R bound to CK1‐7 (Chijiwa et al, 1989; Xu et al, 1996) and C. glabrata Hrr251–403 K38R bound to ADP, with domains colored as in (A). Bound PO4−/SO4− ions are shown as spheres (see Fig EV2A for additional C. glabrata Hrr25 structures and Fig EV3A for SO4− ion electron density).
  3. Overlay of the kinase domain of C. glabrata Hrr25 (Apo form, crystallized with 1.2 M PO4−) with rat CK1δ crystallized in the presence of tungstate ions (WO4; PDB ID 1CKJ; Longenecker et al, 1996) (see Fig EV2B for detailed views of ion binding).
  4. Stereo view of CK1‐7 binding to S. cerevisiae Hrr25. Bound drug is positioned identically to a previous structure of S. pombe Cki1 bound to CK1‐7 (Xu et al, 1996). All active‐site residues shown are conserved between S. cerevisiae and C. glabrata Hrr25.
  5. Stereo view of ADP binding to C. glabrata Hrr25 (formate structure; SO4− structure is equivalent, but the GxGxxG motif is disordered in that structure). All active‐site residues shown are conserved between S. cerevisiae and Candida glabrata Hrr25.