1NBF

Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde

Summary for 1NBF

• Entry DOI: 10.2210/pdb1nbf/pdb
• Related: 1NB8
• Descriptor: Ubiquitin carboxyl-terminal hydrolase 7, Ubiquitin aldehyde (3 entities in total)
• Functional Keywords: deubiquitinating enzyme, hausp, ubiquitin binding, catalytic mechanisms of upbs, hydrolase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 5
• Total formula weight: 140134.68

Authors

Hu, M.,Li, P.,Li, M.,Li, W.,Yao, T.,Wu, J.-W.,Gu, W.,Cohen, R.E.,Shi, Y. (deposition date: 2002-12-02, release date: 2003-01-07, Last modification date: 2025-03-26)

Primary citation

Hu, M.,Li, P.,Li, M.,Li, W.,Yao, T.,Wu, J.-W.,Gu, W.,Cohen, R.E.,Shi, Y.
Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
Cell(Cambridge,Mass.), 111:1041-1054, 2002

PubMed 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.

PubMed: 12507430
DOI: 10.1016/S0092-8674(02)01199-6

Experimental method

X-RAY DIFFRACTION (2.3 Å)