6UYO

Crystal structure of K37-acetylated SUMO1 in complex with PML-SIM

Summary for 6UYO

• Entry DOI: 10.2210/pdb6uyo/pdb
• Related: 4WJN 4WJO 4WJP 4WJQ
• Descriptor: Small ubiquitin-related modifier 1, Protein PML (3 entities in total)
• Functional Keywords: sumo1, pml, sumo interaction motif, nuclear protein-protein binding complex, nuclear protein/protein binding
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 25089.57

Authors

Wahba, H.M.,Gagnon, C.,Mascle, X.H.,Lussier-Price, M.,Sakaguchi, K.,Omichinski, J.G. (deposition date: 2019-11-14, release date: 2019-11-27, Last modification date: 2024-10-30)

Primary citation

Mascle, X.H.,Gagnon, C.,Wahba, H.M.,Lussier-Price, M.,Cappadocia, L.,Sakaguchi, K.,Omichinski, J.G.
Acetylation of SUMO1 Alters Interactions with the SIMs of PML and Daxx in a Protein-Specific Manner.
Structure, 28:157-168.e5, 2020

PubMed Abstract: The interactions between SUMO proteins and SUMO-interacting motif (SIM) in nuclear bodies formed by the promyelocytic leukemia (PML) protein (PML-NBs) have been shown to be modulated by either phosphorylation of the SIMs or acetylation of SUMO proteins. However, little is known about how this occurs at the atomic level. In this work, we examined the role that acetylation of SUMO1 plays on its binding to the phosphorylated SIMs (phosphoSIMs) of PML and Daxx. Our results demonstrate that SUMO1 binding to the phosphoSIM of either PML or Daxx is dramatically reduced by acetylation at either K39 or K46. However, acetylation at K37 only impacts binding to Daxx. Structures of acetylated SUMO1 variants bound to the phosphoSIMs of PML and Daxx demonstrate that there is structural plasticity in SUMO-SIM interactions. The plasticity observed in these structures provides a robust mechanism for regulating SUMO-SIM interactions in PML-NBs using signaling generated post-translational modifications.

PubMed: 31879127
DOI: 10.1016/j.str.2019.11.019

Experimental method

X-RAY DIFFRACTION (1.639 Å)