PDBsum entry 2kiz

Metal binding protein

PDB id: 2kiz

Contents

Protein chain

69 a.a. *

Metals

_ZN ×2

* Residue conservation analysis

PDB id:

2kiz

Name:

Metal binding protein

Title:

Solution structure of arkadia ring-h2 finger domain

Structure:

E3 ubiquitin-protein ligase arkadia. Chain: a. Synonym: ring finger protein 111. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: rnf111. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

31 models

Authors:

N.G.Kandias,C.T.Chasapis,D.Bentrop,V.Episkopou,G.A.Spyroulias

Key ref:

C.T.Chasapis et al. (2012). NMR-based insights into the conformational and interaction properties of Arkadia RING-H2 E3 Ub ligase. Proteins, 80, 1484-1489. PubMed id: 22411132

Date:

13-May-09 Release date: 19-May-10

Protein chain

Q6ZNA4  (RN111_HUMAN) -  E3 ubiquitin-protein ligase Arkadia from Homo sapiens

Seq: 994 a.a.

Struc: 69 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

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

Proteins 80:1484-1489 (2012)

PubMed id: 22411132

NMR-based insights into the conformational and interaction properties of Arkadia RING-H2 E3 Ub ligase.

C.T.Chasapis, N.G.Kandias, V.Episkopou, D.Bentrop, G.A.Spyroulias.

ABSTRACT

Arkadia (Rnf111), an E3 Ubiquitin (Ub) ligase, amplifies TGF-β signaling responses by targeting for degradation of the negative regulators Smad6/7 and the SnoN/Ski transcriptional repressors when they block the TGF-β effectors Smad2/3. The E3 ligase activity of Arkadia depends on its C-terminal RING-H2 domain that constitutes the docking site for the E2 Ub-conjugating enzyme carrying the activated Ub. We determined the nuclear magnetic resonance solution structure of Arkadia's RING-H2 domain and revealed a (β)ββα fold, fully consistent with the expected "cross-brace" mode of Zn(II)-ligation. In addition, the interaction of the Arkadia RING-H2 domain with its E2 partner enzyme (UbcH5b) was examined through chemical shift perturbation. Proteins 2012. © 2012 Wiley Periodicals, Inc.