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Figure 5.
Figure 5. Structural comparison of the monoubiquitin
binding modes of the Ede1 UBA, Cue2 CUE^14 and Dsk2 UBA^13
domains. (a) A structure-guided multiple sequence alignment of
the Ede1 UBA, Dsk2 UBA and Cue2 CUE domains. Residues in helical
regions are shown in uppercase and in bold font for clarity.
Residues constituting the hydrophobic cores of the respective
domains are shaded in yellow, whereas those that interact with
ubiquitin in the respective complexes are shaded in light blue.
(b) Comparison of the Ede1 UBA domain–ubiquitin (light blue)
and Dsk2 UBA domain–ubiquitin (purple) complexes following a
best-fit superposition of the backbone atoms of residues 1–70
of ubiquitin. (c) Ribbon diagrams of the Ede1 UBA domain (light
blue) and Cue2 CUE domain (magenta)–monoubiquitin complexes
following a best-fit superposition of the polypeptide backbone
encompassing residues 1–70 of ubiquitin.
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