2G45

Co-crystal structure of znf ubp domain from the deubiquitinating enzyme isopeptidase T (isot) in complex with ubiquitin

Summary for 2G45

• Entry DOI: 10.2210/pdb2g45/pdb
• Related: 2G43
• Descriptor: Ubiquitin carboxyl-terminal hydrolase 5, Ubiquitin, ZINC ION, ... (5 entities in total)
• Functional Keywords: ubiquitin, zinc finger, deubiquitinating enzyme, hydrolase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 46506.71

Authors

Reyes-Turcu, F.E.,Horton, J.R.,Mullally, J.E.,Heroux, A.,Cheng, X.,Wilkinson, K.D. (deposition date: 2006-02-21, release date: 2006-04-04, Last modification date: 2023-08-30)

Primary citation

Reyes-Turcu, F.E.,Horton, J.R.,Mullally, J.E.,Heroux, A.,Cheng, X.,Wilkinson, K.D.
The Ubiquitin Binding Domain ZnF UBP Recognizes the C-Terminal Diglycine Motif of Unanchored Ubiquitin.
Cell(Cambridge,Mass.), 124:1197-1208, 2006

PubMed Abstract: Ubiquitin binding proteins regulate the stability, function, and/or localization of ubiquitinated proteins. Here we report the crystal structures of the zinc-finger ubiquitin binding domain (ZnF UBP) from the deubiquitinating enzyme isopeptidase T (IsoT, or USP5) alone and in complex with ubiquitin. Unlike other ubiquitin binding domains, this domain contains a deep binding pocket where the C-terminal diglycine motif of ubiquitin is inserted, thus explaining the specificity of IsoT for an unmodified C terminus on the proximal subunit of polyubiquitin. Mutations in the domain demonstrate that it is required for optimal catalytic activation of IsoT. This domain is present in several other protein families, and the ZnF UBP domain from an E3 ligase also requires the C terminus of ubiquitin for binding. These data suggest that binding the ubiquitin C terminus may be necessary for the function of other proteins.

PubMed: 16564012
DOI: 10.1016/j.cell.2006.02.038

Experimental method

X-RAY DIFFRACTION (1.99 Å)