2LBC

solution structure of tandem UBA of USP13

Summary for 2LBC

• Entry DOI: 10.2210/pdb2lbc/pdb
• NMR Information: BMRB: 17554
• Descriptor: Ubiquitin carboxyl-terminal hydrolase 13 (1 entity in total)
• Functional Keywords: tandem uba of usp13, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 13769.25

Authors

Zhang, Y.,Zhou, C.,Zhou, Z.,Song, A.,Hu, H. (deposition date: 2011-03-29, release date: 2012-03-07, Last modification date: 2024-05-15)

Primary citation

Zhang, Y.,Zhou, C.,Zhou, Z.,Song, A.,Hu, H.
Domain Analysis Reveals That a Deubiquitinating Enzyme USP13 Performs Non-Activating Catalysis for Lys63-Linked Polyubiquitin.
Plos One, 6:e29362-e29362, 2011

PubMed Abstract: Deubiquitination is a reverse process of cellular ubiquitination important for many biological events. Ubiquitin (Ub)-specific protease 13 (USP13) is an ortholog of USP5 implicated in catalyzing hydrolysis of various Ub chains, but its enzymatic properties and catalytic regulation remain to be explored. Here we report studies of the roles of the Ub-binding domains of USP13 in regulatory catalysis by biochemical and NMR structural approaches. Our data demonstrate that USP13, distinct from USP5, exhibits a weak deubiquitinating activity preferring to Lys63-linked polyubiquitin (K63-polyUb) in a non-activation manner. The zinc finger (ZnF) domain of USP13 shares a similar fold with that of USP5, but it cannot bind with Ub, so that USP13 has lost its ability to be activated by free Ub. Substitution of the ZnF domain with that of USP5 confers USP13 the property of catalytic activation. The tandem Ub-associated (UBA) domains of USP13 can bind with different types of diUb but preferentially with K63-linked, providing a possible explanation for the weak activity preferring to K63-polyUb. USP13 can also regulate the protein level of CD3δ in cells, probably depending on its weak deubiquitinating activity and the Ub-binding properties of the UBA domains. Thus, the non-activating catalysis of USP13 for K63-polyUb chains implies that it may function differently from USP5 in cellular deubiquitination processes.

PubMed: 22216260
DOI: 10.1371/journal.pone.0029362

Experimental method

SOLUTION NMR