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. 2015 Mar 5;57(5):887–900. doi: 10.1016/j.molcel.2014.12.039

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© 2015 The Authors

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

PMC Copyright notice

Crystal Structures UCH-L5/DEUBAD Complexes

(A) Constructs used in this study.

(B) RPN13^DEU activates UCH-L5 (UR) while INO80G^DEU inhibits UCH-L5 (UI) in Ub-AMC enzyme kinetics. The CD is slightly more active than FL UCH-L5 (U). See Figure 1A for naming codes. Error bars, SD.

(C) Structure of apo UCH-L5 (3ihr). CD, blue; ULD domain, light blue.

(D) Structure of UCH-L5/INO80G^DEU (INO80G^DEU, orange).

(E) Structure of UCH-L5/RPN13^DEU (RPN13^DEU, green).

(F) Structure of UCH-L5∼Ub-Prg/RPN13^DEU (Ub-Prg, yellow).

(G) The ULDs are found in different conformations across UCH-L5 structures. The CD is transparent for clarity.

(H) RPN13^DEU (green) changes toward an open state upon UCH-L5 complex formation compared to apo RPN13^DEU (gray). Helices α1–4 and the α3-4 loop that undergo the largest changes are colored in darker shades.

(I) Superposition of RPN13^DEU and INO80G^DEU. DEUBAD domains deviate most at FRF hairpin and helix α6. See also Tables 1, S1, S2, and S4 and Figure S1.