7P47

Structure of the E3 ligase Smc5/Nse2 in complex with Ubc9-SUMO thioester mimetic

Summary for 7P47

• Entry DOI: 10.2210/pdb7p47/pdb
• Descriptor: Structural maintenance of chromosomes protein 5, SUMO-conjugating enzyme UBC9, E3 SUMO-protein ligase MMS21, ... (5 entities in total)
• Functional Keywords: sumo e3 ligase activity, dna repair, ligase
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 5
• Total formula weight: 80711.56

Authors

Lascorz, J.,Varejao, N.,Reverter, D. (deposition date: 2021-07-09, release date: 2021-11-24, Last modification date: 2024-01-31)

Primary citation

Varejao, N.,Lascorz, J.,Codina-Fabra, J.,Belli, G.,Borras-Gas, H.,Torres-Rosell, J.,Reverter, D.
Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs.
Nat Commun, 12:7013-7013, 2021

PubMed Abstract: Post-translational modification of proteins by ubiquitin and ubiquitin-like modifiers, such as SUMO, are key events in protein homeostasis or DNA damage response. Smc5/6 is a nuclear multi-subunit complex that participates in the recombinational DNA repair processes and is required in the maintenance of chromosome integrity. Nse2 is a subunit of the Smc5/6 complex that possesses SUMO E3 ligase activity by the presence of a SP-RING domain that activates the E2~SUMO thioester for discharge on the substrate. Here we present the crystal structure of the SUMO E3 ligase Nse2 in complex with an E2-SUMO thioester mimetic. In addition to the interface between the SP-RING domain and the E2, the complex reveals how two SIM (SUMO-Interacting Motif) -like motifs in Nse2 are restructured upon binding the donor and E2-backside SUMO during the E3-dependent discharge reaction. Both SIM interfaces are essential in the activity of Nse2 and are required to cope with DNA damage.

PubMed: 34853311
DOI: 10.1038/s41467-021-27301-9

Experimental method

X-RAY DIFFRACTION (3.314 Å)