PDBsum entry 5hqg

Hydrolase

PDB id: 5hqg

Contents

Protein chain

324 a.a.

Waters ×104

PDB id:

5hqg

Name:

Hydrolase

Title:

Wd40 domain of human e3 ubiquitin ligase cop1 (rfwd2)

Structure:

E3 ubiquitin-protein ligase rfwd2. Chain: a. Synonym: constitutive photomorphogenesis protein 1 homolog,hcop1,ring finger and wd repeat domain protein 2,ring finger protein 200. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: rfwd2, cop1, rnf200. Expressed in: trichoplusia ni. Expression_system_taxid: 7111

Resolution:

2.00Å R-factor: 0.214 R-free: 0.242

Authors:

S.Uljon,S.C.Blacklow

Key ref:

S.Uljon et al. (2016). Structural Basis for Substrate Selectivity of the E3 Ligase COP1. Structure, 24, 687-696. PubMed id: 27041596 DOI: 10.1016/j.str.2016.03.002

Date:

21-Jan-16 Release date: 20-Apr-16

Protein chain

Q8NHY2  (COP1_HUMAN) -  E3 ubiquitin-protein ligase COP1 from Homo sapiens

Seq: 731 a.a.

Struc: 324 a.a.

Enzyme reactions

• Enzyme class: 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: 10.1016/j.str.2016.03.002

Structure 24:687-696 (2016)

PubMed id: 27041596

Structural Basis for Substrate Selectivity of the E3 Ligase COP1.

S.Uljon, X.Xu, I.Durzynska, S.Stein, G.Adelmant, J.A.Marto, W.S.Pear, S.C.Blacklow.

ABSTRACT

COP1 proteins are E3 ubiquitin ligases that regulate phototropism in plants and target transcription factors for degradation in mammals. The substrate-binding region of COP1 resides within a WD40-repeat domain that also binds to Trib proteins, which are adaptors for C/EBPα degradation. Here we report structures of the human COP1 WD40 domain in isolation, and complexes of the human and Arabidopsis thaliana COP1 WD40 domains with the binding motif of Trib1. The human and Arabidopsis WD40 domains are seven-bladed β propellers with an inserted loop on the bottom face of the first blade. The Trib1 peptide binds in an extended conformation to a highly conserved surface on the top face of the β propeller, indicating a general mode for recognition of peptide motifs by COP1. Together, these studies identify the structural basis and key interactions for motif recognition by COP1, and hint at how Trib1 autoinhibition is overcome to target C/EBPα for degradation.