PDBsum entry 6uyu

Nuclear protein/protein binding

PDB id: 6uyu

Contents

Protein chains

79 a.a.

12 a.a.

11 a.a.

Waters ×206

PDB id:

6uyu

Name:

Nuclear protein/protein binding

Title:

Crystal structure of k45-acetylated sumo1 in complex with phosphorylated pml-sim

Structure:

Small ubiquitin-related modifier 1. Chain: a, c. Synonym: sumo-1,gap-modifying protein 1,gmp1,smt3 homolog 3,sentrin, ubiquitin-homology domain protein pic1,ubiquitin-like protein smt3c, smt3c,ubiquitin-like protein ubl1. Engineered: yes. Mutation: yes. Protein pml. Chain: b, d.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: sumo1, smt3c, smt3h3, ubl1, ok/sw-cl.43. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: pml, myl, pp8675, rnf71, trim19. Expression_system_taxid: 562

Resolution:

1.66Å R-factor: 0.171 R-free: 0.186

Authors:

H.M.Wahba,C.Gagnon,X.H.Mascle,M.Lussier-Price,L.Cappadocia, K.Sakaguchi,J.G.Omichinski

Key ref:

X.H.Mascle et al. (2020). Acetylation of SUMO1 Alters Interactions with the SIMs of PML and Daxx in a Protein-Specific Manner. Structure, 28, 157. PubMed id: 31879127 DOI: 10.1016/j.str.2019.11.019

Date:

14-Nov-19 Release date: 27-Nov-19

Protein chains

P63165  (SUMO1_HUMAN) -  Small ubiquitin-related modifier 1 from Homo sapiens

Seq: 101 a.a.

Struc: 79 a.a.*

Protein chain

P29590  (PML_HUMAN) -  Protein PML from Homo sapiens

Seq: 882 a.a.

Struc: 12 a.a.

Protein chain

P29590  (PML_HUMAN) -  Protein PML from Homo sapiens

Seq: 882 a.a.

Struc: 11 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains B, D: E.C.2.3.2.- - ?????

DOI no: 10.1016/j.str.2019.11.019

Structure 28:157 (2020)

PubMed id: 31879127

Acetylation of SUMO1 Alters Interactions with the SIMs of PML and Daxx in a Protein-Specific Manner.

X.H.Mascle, C.Gagnon, H.M.Wahba, M.Lussier-Price, L.Cappadocia, K.Sakaguchi, J.G.Omichinski.

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.