6V7S

Crystal structure of K37-acetylated SUMO1 in complex with phosphorylated PIAS-SIM2

Summary for 6V7S

• Entry DOI: 10.2210/pdb6v7s/pdb
• Related: 6V7P 6V7Q 6V7R
• Descriptor: Small ubiquitin-related modifier 1, Protein PIAS (3 entities in total)
• Functional Keywords: sumo1, pias, sumo interaction motif, peptide binding protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 22048.46

Authors

Lussier-Price, M.,Wahba, H.M.,Mascle, X.H.,Cappadocia, L.,Sakaguchi, K.,Omichinski, J.G. (deposition date: 2019-12-09, release date: 2020-04-01, Last modification date: 2024-11-06)

Primary citation

Lussier-Price, M.,Mascle, X.H.,Cappadocia, L.,Kamada, R.,Sakaguchi, K.,Wahba, H.M.,Omichinski, J.G.
Characterization of a C-Terminal SUMO-Interacting Motif Present in Select PIAS-Family Proteins.
Structure, 28:573-585.e5, 2020

PubMed Abstract: The human PIAS proteins are small ubiquitin-like modifier (SUMO) E3 ligases that participate in important cellular functions. Several of these functions depend on a conserved SUMO-interacting motif (SIM) located in the central region of all PIAS proteins (SIM1). Recently, it was determined that Siz2, a yeast homolog of PIAS proteins, possesses a second SIM at its C terminus (SIM2). Sequence alignment indicates that a SIM2 is also present in PIAS1-3, but not PIAS4. Using biochemical and structural studies, we demonstrate PIAS-SIM2 binds to SUMO1, but that phosphorylation of the PIAS-SIM2 or acetylation of SUMO1 alter this interaction in a manner distinct from what is observed for the PIAS-SIM1. We also show that the PIAS-SIM2 plays a key role in formation of a UBC9-PIAS1-SUMO1 complex. These results provide insights into how post-translational modifications selectively regulate the specificity of multiple SIMs found in the PIAS proteins by exploiting the plasticity built into the SUMO-SIM binding interface.

PubMed: 32348746
DOI: 10.1016/j.str.2020.04.002

Experimental method

X-RAY DIFFRACTION (1.47 Å)