Abstract:
:The ubiquitin-specific processing protease (UBP) family of deubiquitinating enzymes plays an essential role in numerous cellular processes. HAUSP, a representative UBP, specifically deubiquitinates and hence stabilizes the tumor suppressor protein p53. Here, we report the crystal structures of the 40 kDa catalytic core domain of HAUSP in isolation and in complex with ubiquitin aldehyde. These studies reveal that the UBP deubiquitinating enzymes exhibit a conserved three-domain architecture, comprising Fingers, Palm, and Thumb. The leaving ubiquitin moiety is specifically coordinated by the Fingers, with its C terminus placed in the active site between the Palm and the Thumb. Binding by ubiquitin aldehyde induces a drastic conformational change in the active site that realigns the catalytic triad residues for catalysis.
journal_name
Celljournal_title
Cellauthors
Hu M,Li P,Li M,Li W,Yao T,Wu JW,Gu W,Cohen RE,Shi Ydoi
10.1016/s0092-8674(02)01199-6subject
Has Abstractpub_date
2002-12-27 00:00:00pages
1041-54issue
7eissn
0092-8674issn
1097-4172pii
S0092867402011996journal_volume
111pub_type
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