PDBsum entry 4jgh

Ligase

PDB id: 4jgh

Contents

Protein chains

163 a.a.

104 a.a.

96 a.a.

368 a.a.

PDB id:

4jgh

Name:

Ligase

Title:

Structure of the socs2-elongin bc complex bound to an n-terminal fragment of cullin5

Structure:

Suppressor of cytokine signaling 2. Chain: a. Fragment: unp residues 32-198. Synonym: socs-2, cytokine-inducible sh2 protein 2, cis-2, stat- induced stat inhibitor 2, ssi-2. Engineered: yes. Transcription elongation factor b polypeptide 2. Chain: b. Synonym: elongin 18 kda subunit, elongin-b, elob, RNA polymerase ii

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: cis2, homo sapiens, socs2, ssi2, stati2. Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. Mouse. Organism_taxid: 10090.

Resolution:

3.00Å R-factor: 0.225 R-free: 0.248

Authors:

Y.K.Kim,M.J.Kwak,B.Ku,H.Y.Suh,K.Joo,J.Lee,J.U.Jung,B.H.Oh

Key ref:

Y.K.Kim et al. (2013). Structural basis of intersubunit recognition in elongin BC-cullin 5-SOCS box ubiquitin-protein ligase complexes. Acta Crystallogr D Biol Crystallogr, 69, 1587-1597. PubMed id: 23897481 DOI: 10.1107/S0907444913011220

Date:

01-Mar-13 Release date: 07-Aug-13

Protein chain

O14508  (SOCS2_HUMAN) -  Suppressor of cytokine signaling 2 from Homo sapiens

Seq: 198 a.a.

Struc: 163 a.a.*

Protein chain

P62869  (ELOB_MOUSE) -  Elongin-B from Mus musculus

Seq: 118 a.a.

Struc: 104 a.a.

Protein chain

P83940  (ELOC_MOUSE) -  Elongin-C from Mus musculus

Seq: 112 a.a.

Struc: 96 a.a.*

Protein chain

Q93034  (CUL5_HUMAN) -  Cullin-5 from Homo sapiens

Seq: 780 a.a.

Struc: 368 a.a.*

* PDB and UniProt seqs differ at 9 residue positions (black crosses)

DOI no: 10.1107/S0907444913011220

Acta Crystallogr D Biol Crystallogr 69:1587-1597 (2013)

PubMed id: 23897481

Structural basis of intersubunit recognition in elongin BC-cullin 5-SOCS box ubiquitin-protein ligase complexes.

Y.K.Kim, M.J.Kwak, B.Ku, H.Y.Suh, K.Joo, J.Lee, J.U.Jung, B.H.Oh.

ABSTRACT

The cullin-RING ubiquitin ligases are multisubunit complexes that ubiquitinate various proteins. Six different cullins encoded by the human genome selectively pair with different adaptors and substrate receptors. It is presently poorly understood how cullin-2 (Cul2) and cullin-5 (Cul5) associate specifically with their adaptor elongin BC and a SOCS-box-containing substrate receptor. Here, crystallographic and mutational analyses of a quaternary complex between the N-terminal half of Cul5, elongin BC and SOCS2 are reported. Cul5 interacts extensively with elongin BC via residues that are highly conserved in Cul2 but not in other cullins. Cul5 also interacts with SOCS2, but via only two residues, Pro184 and Arg186, which are located in the C-terminal part of the SOCS box called the Cul5 box. Pro184 makes a ring-to-ring interaction with Trp53 of Cul5, which is substituted by alanine in Cul2. This interaction is shown to contribute significantly to the overall binding affinity between Cul5 and SOCS2-elongin BC. This study provides structural bases underlying the specificity of Cul5 and Cul2 for elongin BC and their preferential association with Cul5 or Cul2 box-containing substrate receptors.