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![[Figure 2]](nj5320fig2mag.jpg)
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Figure 2
Structure of the disulfide-linked SdeA DUB–UbG76C complex. (a) SDS–PAGE (nonreducing) analysis of a purified sample of SdeA DUB in a disulfide-linked complex with UbG76C. (a) Ribbon representation of the crystal structure of the disulfide-linked complex of UbG76C (slate) and SdeA (raspberry). Right: enlargement of the boxed region shows that there is continuous electron density (2Fo − Fc at 1σ) between the C-terminal cysteine of UbG76C and the catalytic cysteine of SdeA DUB. (c) Catalytic triad of SdeA DUB compared between the disulfide-linked structure, the Ub-VME-bound structure (lime green) and the apo structure (PDB entry 5crb, C118A mutant; orange). (d) Superposition of the Ub-VME-bound structure (green) and the disulfide-linked SdeA DUB–Ub complex structure (raspberry). The G76C residue is highlighted in stick representation in slate. The movement of the catalytic cysteine and the unfurling of a helical turn (that carries the catalytic cysteine) to accommodate the disulfide bridge between Cys76 of Ub and Cys118 of SdeA is shown by an arrow. The cysteine (green sticks) in the SdeA DUB–Ub-VME complex represents its native-like conformation. |
![[Figure 2]](nj5320fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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