3M99

Structure of the Ubp8-Sgf11-Sgf73-Sus1 SAGA DUB module

Summary for 3M99

• Entry DOI: 10.2210/pdb3m99/pdb
• Descriptor: Ubiquitin carboxyl-terminal hydrolase 8, SAGA-associated factor 11, Protein SUS1, ... (6 entities in total)
• Functional Keywords: zinc finger, activator, chromatin regulator, metal-binding, nucleus, transcription, transcription regulation, zinc-finger, mrna transport, ubiquitination, deubiquitination, nuclear pore complex, protein modification
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); More
• Cellular location: Nucleus : P50102 Q03067 P53165; Nucleus, nucleoplasm: Q6WNK7
• Total number of polymer chains: 4
• Total formula weight: 88080.34

Authors

Kohler, A.,Zimmerman, E.,Schneider, M.,Hurt, E.,Zheng, N. (deposition date: 2010-03-21, release date: 2010-05-05, Last modification date: 2024-10-16)

Primary citation

Kohler, A.,Zimmerman, E.,Schneider, M.,Hurt, E.,Zheng, N.
Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module.
Cell(Cambridge,Mass.), 141:606-617, 2010

PubMed Abstract: Deubiquitinating enzymes (DUBs) regulate diverse cellular functions by cleaving ubiquitin from specific protein substrates. How their activities are modulated in various cellular contexts remains poorly understood. The yeast deubiquitinase Ubp8 protein is recruited and activated by the SAGA complex and, together with Sgf11, Sus1, and Sgf73, forms a DUB module responsible for deubiquitinating histone H2B during gene expression. Here, we report the crystal structure of the complete SAGA DUB module, which features two functional lobes structurally coupled by Sgf73. In the "assembly lobe," a long Sgf11 N-terminal helix is clamped onto the Ubp8 ZnF-UBP domain by Sus1. In the "catalytic lobe," an Sgf11 C-terminal zinc-finger domain binds to the Ubp8 catalytic domain next to its active site. Our structural and functional analyses reveal a central role of Sgf11 and Sgf73 in activating Ubp8 for deubiquitinating histone H2B and demonstrate how a DUB can be allosterically regulated by its nonsubstrate partners.

PubMed: 20434206
DOI: 10.1016/j.cell.2010.04.026

Experimental method

X-RAY DIFFRACTION (2.7 Å)