PDBsum entry 5jg6

Cell cycle

PDB id: 5jg6

Contents

Protein chains

61 a.a.

77 a.a.

66 a.a.

Metals

_ZN ×6

Waters ×116

PDB id:

5jg6

Name:

Cell cycle

Title:

Apc11-ubv shows role of noncovalent ring-ubiquitin interactions in processive multiubiquitination and ubiquitin chain elongation by apc/c

Structure:

Anaphase-promoting complex subunit 11. Chain: a, d. Synonym: apc11,cyclosome subunit 11,hepatocellular carcinoma- associated ring finger protein. Engineered: yes. Polyubiquitin-b. Chain: b, c. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: anapc11, hspc214. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ubb. Expression_system_taxid: 562

Resolution:

2.00Å R-factor: 0.187 R-free: 0.220

Authors:

N.G.Brown,W.Zhang,S.Yu,D.J.Miller,S.S.Sidhu,B.A.Schulman

Key ref:

N.G.Brown et al. (2016). Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. Cell, 165, 1440-1453. PubMed id: 27259151 DOI: 10.1016/j.cell.2016.05.037

Date:

19-Apr-16 Release date: 15-Jun-16

Protein chain

Q9NYG5  (APC11_HUMAN) -  Anaphase-promoting complex subunit 11 from Homo sapiens

Seq: 84 a.a.

Struc: 61 a.a.

Protein chains

P0CG47  (UBB_HUMAN) -  Polyubiquitin-B from Homo sapiens

Seq: 229 a.a.

Struc: 77 a.a.*

Protein chain

Q9NYG5  (APC11_HUMAN) -  Anaphase-promoting complex subunit 11 from Homo sapiens

Seq: 84 a.a.

Struc: 66 a.a.

* PDB and UniProt seqs differ at 15 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B, C, D: E.C.?

DOI no: 10.1016/j.cell.2016.05.037

Cell 165:1440-1453 (2016)

PubMed id: 27259151

Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C.

N.G.Brown, R.VanderLinden, E.R.Watson, F.Weissmann, A.Ordureau, K.P.Wu, W.Zhang, S.Yu, P.Y.Mercredi, J.S.Harrison, I.F.Davidson, R.Qiao, Y.Lu, P.Dube, M.R.Brunner, C.R.Grace, D.J.Miller, D.Haselbach, M.A.Jarvis, M.Yamaguchi, D.Yanishevski, G.Petzold, S.S.Sidhu, B.Kuhlman, M.W.Kirschner, J.W.Harper, J.M.Peters, H.Stark, B.A.Schulman.

ABSTRACT

Protein ubiquitination involves E1, E2, and E3 trienzyme cascades. E2 and RING E3 enzymes often collaborate to first prime a substrate with a single ubiquitin (UB) and then achieve different forms of polyubiquitination: multiubiquitination of several sites and elongation of linkage-specific UB chains. Here, cryo-EM and biochemistry show that the human E3 anaphase-promoting complex/cyclosome (APC/C) and its two partner E2s, UBE2C (aka UBCH10) and UBE2S, adopt specialized catalytic architectures for these two distinct forms of polyubiquitination. The APC/C RING constrains UBE2C proximal to a substrate and simultaneously binds a substrate-linked UB to drive processive multiubiquitination. Alternatively, during UB chain elongation, the RING does not bind UBE2S but rather lures an evolving substrate-linked UB to UBE2S positioned through a cullin interaction to generate a Lys11-linked chain. Our findings define mechanisms of APC/C regulation, and establish principles by which specialized E3-E2-substrate-UB architectures control different forms of polyubiquitination.