PDBsum entry 4y1h

Signaling protein

PDB id: 4y1h

Contents

Protein chain

76 a.a.

Ligands

EDO ×4

Waters ×36

PDB id:

4y1h

Name:

Signaling protein

Title:

Crystal structure of k33 linked tri-ubiquitin

Structure:

Ubiquitin-40s ribosomal protein s27a. Chain: a. Synonym: ubiquitin carboxyl extension protein 80. Other_details: k33 linked tri-ubiquitin.

Source:

Bos taurus. Cattle. Organism_taxid: 9913

Resolution:

1.40Å R-factor: 0.160 R-free: 0.194

Authors:

Y.A.Kristariyanto,S.A.Abdul Rehman,S.Y.Choi,S.Ritorto,D.G.Campbell, N.A.Morrice,R.Toth,Y.Kulathu

Key ref:

Y.A.Kristariyanto et al. (2015). Assembly and structure of Lys33-linked polyubiquitin reveals distinct conformations. Biochem J, 467, 345-352. PubMed id: 25723849 DOI: 10.1042/BJ20141502

Date:

07-Feb-15 Release date: 18-Mar-15

Protein chain

P62992  (RS27A_BOVIN) -  Ubiquitin-ribosomal protein eS31 fusion protein from Bos taurus

Seq: 156 a.a.

Struc: 76 a.a.

DOI no: 10.1042/BJ20141502

Biochem J 467:345-352 (2015)

PubMed id: 25723849

Assembly and structure of Lys33-linked polyubiquitin reveals distinct conformations.

Y.A.Kristariyanto, S.Y.Choi, S.A.Rehman, M.S.Ritorto, D.G.Campbell, N.A.Morrice, R.Toth, Y.Kulathu.

ABSTRACT

Ubiquitylation regulates a multitude of biological processes and this versatility stems from the ability of ubiquitin (Ub) to form topologically different polymers of eight different linkage types. Whereas some linkages have been studied in detail, other linkage types including Lys33-linked polyUb are poorly understood. In the present study, we identify an enzymatic system for the large-scale assembly of Lys33 chains by combining the HECT (homologous to the E6-AP C-terminus) E3 ligase AREL1 (apoptosis-resistant E3 Ub protein ligase 1) with linkage selective deubiquitinases (DUBs). Moreover, this first characterization of the chain selectivity of AREL1 indicates its preference for assembling Lys33- and Lys11-linked Ub chains. Intriguingly, the crystal structure of Lys33-linked diUb reveals that it adopts a compact conformation very similar to that observed for Lys11-linked diUb. In contrast, crystallographic analysis of Lys33-linked triUb reveals a more extended conformation. These two distinct conformational states of Lys33-linked polyUb may be selectively recognized by Ub-binding domains (UBD) and enzymes of the Ub system. Importantly, our work provides a method to assemble Lys33-linked polyUb that will allow further characterization of this atypical chain type.