journal menu
![[Figure 3]](nj5320fig3mag.jpg)
|
|
Figure 3
Interactions with Ub are preserved in the disulfide-linked structure. (a) Superposition of the SdeA DUB complex with Ub in the disulfide-linked form (raspberry and slate), the Ub-VME-bound form (green and yellow) and the Ub product-bound form (pink and orange). The C-terminal tail of Ub (from Leu71 to Gly75) is shown as sticks. Active-site SdeA DUB residues that form β-sheet-like interactions with the tail are shown as raspberry sticks. The hydrogen-bond network formed between the C-terminal tail of Ub and SdeA DUB is indicated as dashed lines. The red boxes indicate the regions depicted in (c). The numbering of the boxes corresponds to the numbering in (c). (b) Left: the hydrogen bond (dashed line) between SdeA DUB residues Glu9 and Ser62 is conserved in the VME-bound, product-bound and disulfide-bound structures. Right: in the apo form of SdeA DUB (orange) this interaction is not observed, indicating an open active site. (c) Hydrogen-bonding interactions (dashed lines) in other areas distal to the active site that were observed between Ub and SdeA DUB in the Ub-VME-bound and product-bound structures are maintained in the disulfide-linked structure. |
![[Figure 3]](nj5320fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Open 
access
access
