PDBsum entry 2n9p

Ligase

PDB id: 2n9p

Contents

Protein chains

42 a.a.

100 a.a.

Metals

_ZN

PDB id:

2n9p

Name:

Ligase

Title:

Solution structure of rnf126 n-terminal zinc finger domain in complex with bag6 ubiquitin-like domain

Structure:

E3 ubiquitin-protein ligase rnf126. Chain: a. Fragment: n-terminal zinc finger domain residues 1-40. Synonym: ring finger protein 126. Engineered: yes. Large proline-rich protein bag6. Chain: c. Fragment: ubiquitin-like domain, residues 17-101. Synonym: bag family molecular chaperone regulator 6, bcl2-associated

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: rnf126. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: bag6, bat3, g3.

NMR struc:

20 models

Authors:

S.Martinez-Lumbreras,E.M.Krysztofinska,A.Thapaliya,R.L.Isaacson

Key ref:

E.M.Krysztofinska et al. (2016). Structural and functional insights into the E3 ligase, RNF126. Sci Rep, 6, 26433. PubMed id: 27193484 DOI: 10.1038/srep26433

Date:

01-Dec-15 Release date: 25-May-16

Protein chain

Q9BV68  (RN126_HUMAN) -  E3 ubiquitin-protein ligase RNF126 from Homo sapiens

Seq: 311 a.a.

Struc: 42 a.a.

Protein chain

P46379  (BAG6_HUMAN) -  Large proline-rich protein BAG6 from Homo sapiens

Seq: 1132 a.a.

Struc: 100 a.a.*

* PDB and UniProt seqs differ at 13 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chain A: 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

DOI no: 10.1038/srep26433

Sci Rep 6:26433 (2016)

PubMed id: 27193484

Structural and functional insights into the E3 ligase, RNF126.

E.M.Krysztofinska, S.Martínez-Lumbreras, A.Thapaliya, N.J.Evans, S.High, R.L.Isaacson.

ABSTRACT

RNF126 is an E3 ubiquitin ligase that collaborates with the BAG6 sortase complex to ubiquitinate hydrophobic substrates in the cytoplasm that are destined for proteasomal recycling. Composed of a trimeric complex of BAG6, TRC35 and UBL4A the BAG6 sortase is also associated with SGTA, a co-chaperone from which it can obtain hydrophobic substrates. Here we solve the solution structure of the RNF126 zinc finger domain in complex with the BAG6 UBL domain. We also characterise an interaction between RNF126 and UBL4A and analyse the competition between SGTA and RNF126 for the N-terminal BAG6 binding site. This work sheds light on the sorting mechanism of the BAG6 complex and its accessory proteins which, together, decide the fate of stray hydrophobic proteins in the aqueous cytoplasm.