PDBsum entry 2mp2

Protein binding

PDB id: 2mp2

Contents

Protein chains

82 a.a.

90 a.a.

25 a.a.

PDB id:

2mp2

Name:

Protein binding

Title:

Solution structure of sumo dimer in complex with sim2-3 from rnf4

Structure:

Small ubiquitin-related modifier 3. Chain: a. Fragment: unp residues 12-92. Synonym: sumo-3, smt3 homolog 1, sumo-2, ubiquitin-like protein smt3b, smt3b. Engineered: yes. Small ubiquitin-related modifier 3. Chain: b. Fragment: unp residues 2-90.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: smt3b, smt3h1, sumo3. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Mus musculus. Mouse.

NMR struc:

10 models

Authors:

Y.Xu,A.Plechanovov,P.Simpson,J.Marchant,O.Leidecker,K.Sebastian, R.T.Hay,S.J.Matthews

Key ref:

Y.Xu et al. (2014). Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4. Nat Commun, 5, 4217. PubMed id: 24969970 DOI: 10.1038/ncomms5217

Date:

09-May-14 Release date: 02-Jul-14

Protein chain

P55854  (SUMO3_HUMAN) -  Small ubiquitin-related modifier 3 from Homo sapiens

Seq: 103 a.a.

Struc: 82 a.a.*

Protein chain

P55854  (SUMO3_HUMAN) -  Small ubiquitin-related modifier 3 from Homo sapiens

Seq: 103 a.a.

Struc: 90 a.a.*

Protein chain

Q9QZS2  (RNF4_MOUSE) -  E3 ubiquitin-protein ligase RNF4 from Mus musculus

Seq: 194 a.a.

Struc: 25 a.a.

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

Enzyme reactions

• Enzyme class 2: Chains A, B: E.C.?
• Enzyme class 3: Chain C: E.C.2.3.2.27 - RING-type E3 ubiquitin transferase.
• Reaction: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N₆- ubiquitinyl-[acceptor protein]-L-lysine

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

DOI no: 10.1038/ncomms5217

Nat Commun 5:4217 (2014)

PubMed id: 24969970

Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4.

Y.Xu, A.Plechanovová, P.Simpson, J.Marchant, O.Leidecker, S.Kraatz, R.T.Hay, S.J.Matthews.

ABSTRACT

The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response. The SUMO-targeted ubiquitin ligase RNF4 engages with SUMO chains on linked substrates and catalyses their ubiquitination, which targets substrates for proteasomal degradation. Here we use a segmental labelling approach combined with solution nuclear magnetic resonance (NMR) spectroscopy and biochemical characterization to reveal how RNF4 manipulates the conformation of the SUMO chain, thereby facilitating optimal delivery of the distal SUMO domain for ubiquitin transfer.