3I2D

Crystal Structure of S. Cerevisiae SUMO E3 Ligase SIZ1

Summary for 3I2D

• Entry DOI: 10.2210/pdb3i2d/pdb
• Descriptor: E3 SUMO-protein ligase SIZ1, ZINC ION (3 entities in total)
• Functional Keywords: sumo, signal transduction, replication, ring e3, pias, siz, ubiquitin, ubc9, ligase, metal-binding, nucleus, phosphoprotein, ubl conjugation pathway, zinc-finger
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Cytoplasm, cytosol: Q04195
• Total number of polymer chains: 1
• Total formula weight: 41762.65

Authors

Lima, C.D.,Yunus, A.A. (deposition date: 2009-06-29, release date: 2009-09-15, Last modification date: 2024-02-21)

Primary citation

Yunus, A.A.,Lima, C.D.
Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA.
Mol.Cell, 35:669-682, 2009

PubMed Abstract: Siz1 is a founding member of the Siz/PIAS RING family of SUMO E3 ligases. The X-ray structure of an active Siz1 ligase revealed an elongated tripartite architecture comprised of an N-terminal PINIT domain, a central zinc-containing RING-like SP-RING domain, and a C-terminal domain we term the SP-CTD. Structure-based mutational analysis and biochemical studies show that the SP-RING and SP-CTD are required for activation of the E2 approximately SUMO thioester, while the PINIT domain is essential for redirecting SUMO conjugation to the proliferating cell nuclear antigen (PCNA) at lysine 164, a nonconsensus lysine residue that is not modified by the SUMO E2 in the absence of Siz1. Mutational analysis of Siz1 and PCNA revealed surfaces on both proteins that are required for efficient SUMO modification of PCNA in vitro and in vivo.

PubMed: 19748360
DOI: 10.1016/j.molcel.2009.07.013

Experimental method

X-RAY DIFFRACTION (2.6 Å)