PDBsum entry 4wjp

Protein binding/signaling protein

PDB id: 4wjp

Contents

Protein chains

79 a.a.

11 a.a.

12 a.a.

Waters ×177

PDB id:

4wjp

Name:

Protein binding/signaling protein

Title:

Crystal structure of sumo1 in complex with phosphorylated daxx

Structure:

Small ubiquitin-related modifier 1. Chain: a, c. Fragment: unp residues 17-97. 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. Daxx.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: sumo1, smt3c, smt3h3, ubl1, ok/sw-cl.43. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606

Resolution:

1.70Å R-factor: 0.165 R-free: 0.195

Authors:

L.Cappadocia,X.H.Mascle,V.Bourdeau,S.Tremblay-Belzile,M.Chaker- Margot,M.Lussier-Price,J.Wada,K.Sakaguchi,M.Aubry,G.Ferbeyre, J.G.Omichinski

Key ref:

L.Cappadocia et al. (2015). Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1. Structure, 23, 126-138. PubMed id: 25497731 DOI: 10.1016/j.str.2014.10.015

Date:

01-Oct-14 Release date: 31-Dec-14

Protein chains

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

Seq: 101 a.a.

Struc: 79 a.a.*

Protein chain

No UniProt id for this chain

Struc: 11 a.a.

Protein chain

No UniProt id for this chain

Struc: 12 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1016/j.str.2014.10.015

Structure 23:126-138 (2015)

PubMed id: 25497731

Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1.

L.Cappadocia, X.H.Mascle, V.Bourdeau, S.Tremblay-Belzile, M.Chaker-Margot, M.Lussier-Price, J.Wada, K.Sakaguchi, M.Aubry, G.Ferbeyre, J.G.Omichinski.

ABSTRACT

PML and several other proteins localizing in PML-nuclear bodies (PML-NB) contain phosphoSIMs (SUMO-interacting motifs), and phosphorylation of this motif plays a key role in their interaction with SUMO family proteins. We examined the role that phosphorylation plays in the binding of the phosphoSIMs of PML and Daxx to SUMO1 at the atomic level. The crystal structures of SUMO1 bound to unphosphorylated and tetraphosphorylated PML-SIM peptides indicate that three phosphoserines directly contact specific positively charged residues of SUMO1. Surprisingly, the crystal structure of SUMO1 bound to a diphosphorylated Daxx-SIM peptide indicate that the hydrophobic residues of the phosphoSIM bind in a manner similar to that seen with PML, but important differences are observed when comparing the phosphorylated residues. Together, the results provide an atomic level description of how specific acetylation patterns within different SUMO family proteins can work together with phosphorylation of phosphoSIM's regions of target proteins to regulate binding specificity.