2HD5: Usp2 In Complex With Ubiquitin

Citation:
Abstract
Deubiquitinating proteases reverse protein ubiquitination and rescue their target proteins from destruction by the proteasome. USP2, a cysteine protease and a member of the ubiquitin specific protease family, is overexpressed in prostate cancer and stabilizes fatty acid synthase, which has been associated with the malignancy of some aggressive prostate cancers. Here, we report the structure of the human USP2 catalytic domain in complex with ubiquitin. Ubiquitin uses two major sites for the interaction with the protease. Both sites are required simultaneously, as shown by USP2 inhibition assays with peptides and ubiquitin mutants. In addition, a layer of ordered water molecules mediates key interactions between ubiquitin and USP2. As several of those molecules are found at identical positions in the previously solved USP7/ubiquitin-aldehyde complex structure, we suggest a general mechanism of water-mediated ubiquitin recognition by USPs.
PDB ID: 2HD5Download
MMDB ID: 41035
PDB Deposition Date: 2006/6/20
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 1.85  Å
Source Organism:
Bos taurus
Similar Structures:
Biological Unit for 2HD5: dimeric; determined by author and by software (PISA)
Molecular Components in 2HD5
Label Count Molecule
Proteins (2 molecules)
1
Ubiquitin Carboxyl-terminal Hydrolase 2(Gene symbol: USP2)
Molecule annotation
1
Polyubiquitin
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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