The crystal structure of S. cerevisiae Sad1, a catalytically inactive deubiquitinase that is broadly required for pre-mRNA splicing

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FIGURE 3.
FIGURE 3.

The crystal structure of full-length Sad1. (A) The ZnF-UBP (pale orange) and the iUSP domain (slate blue) are connected through a 25-amino-acid linker (pale green). (B) Intradomain hydrogen bonding of K199 to D43 and of K207 to D41 provides interdomain stabilization. (C) Intradomain hydrophobic packing between F206, L140, R37, and a hydrophobic patch on the ZnF-UBP domain further specifies the orientation of the two domains.

This Article

  1. Published in Advance March 28, 2014, doi: 10.1261/rna.042838.113 RNA 20: 656-669

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