PDBsum entry 5ln1

Ubiquitin-binding protein

PDB id: 5ln1

Contents

Protein chains

188 a.a.

76 a.a.

PDB id:

5ln1

Name:

Ubiquitin-binding protein

Title:

Structure of ubiquitylated-rpn10 from yeast;

Structure:

26s proteasome regulatory subunit rpn10. Chain: a. Fragment: unp residues 1-191. Engineered: yes. Polyubiquitin-b. Chain: u. Engineered: yes

Source:

Saccharomyces cerevisiae (strain atcc 204508 / s288c). Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: rpn10, mcb1, sun1, yhr200w. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens.

Resolution:

3.14Å R-factor: 0.193 R-free: 0.248

Authors:

T.Keren-Kaplan,I.Attali,O.Levin-Kravets,G.Prag

Key ref:

T.Keren-Kaplan et al. (2016). Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism. Nat Commun, 7, 12960. PubMed id: 27698474

Date:

02-Aug-16 Release date: 19-Oct-16

Protein chain

P38886  (RPN10_YEAST) -  26S proteasome regulatory subunit RPN10 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 268 a.a.

Struc: 188 a.a.

Protein chain

P0CG47  (UBB_HUMAN) -  Polyubiquitin-B from Homo sapiens

Seq: 229 a.a.

Struc: 76 a.a.

Enzyme reactions

• Enzyme class: Chains A, U: E.C.?

Nat Commun 7:12960 (2016)

PubMed id: 27698474

Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism.

T.Keren-Kaplan, L.Zeev Peters, O.Levin-Kravets, I.Attali, O.Kleifeld, N.Shohat, S.Artzi, O.Zucker, I.Pilzer, N.Reis, M.H.Glickman, S.Ben-Aroya, G.Prag.

ABSTRACT

Ubiquitin receptors decode ubiquitin signals into many cellular responses. Ubiquitin receptors also undergo coupled monoubiquitylation, and rapid deubiquitylation has hampered the characterization of the ubiquitylated state. Using bacteria that express a ubiquitylation apparatus, we purified and determined the crystal structure of the proteasomal ubiquitin-receptor Rpn10 in its ubiquitylated state. The structure shows a novel ubiquitin-binding patch that directs K84 ubiquitylation. Superimposition of ubiquitylated-Rpn10 onto electron-microscopy models of proteasomes indicates that the Rpn10-conjugated ubiquitin clashes with Rpn9, suggesting that ubiquitylation might be involved in releasing Rpn10 from the proteasome. Indeed, ubiquitylation on immobilized proteasomes dissociates the modified Rpn10 from the complex, while unmodified Rpn10 mainly remains associated. In vivo experiments indicate that contrary to wild type, Rpn10-K84R is stably associated with the proteasomal subunit Rpn9. Similarly Rpn10, but not ubiquitylated-Rpn10, binds Rpn9 in vitro. Thus we suggest that ubiquitylation functions to dissociate modified ubiquitin receptors from their targets, a function that promotes cyclic activity of ubiquitin receptors.