PDBsum entry 1yiu

Ligase

PDB id: 1yiu

Contents

Protein chain

37 a.a. *

* Residue conservation analysis

PDB id:

1yiu

Name:

Ligase

Title:

Itch e3 ubiquitin ligase ww3 domain

Structure:

Itchy e3 ubiquitin protein ligase. Chain: a. Fragment: ww3. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Gene: itch e3 ww3 domain. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

8 models

Authors:

A.Z.Shaw,P.Martin-Malpartida,B.Morales,F.Yraola,M.Royo,M.J.Macias

Key ref:

A.Z.Shaw et al. (2005). Phosphorylation of either Ser16 or Thr30 does not disrupt the structure of the Itch E3 ubiquitin ligase third WW domain. Proteins, 60, 558-560. PubMed id: 15971201 DOI: 10.1002/prot.20466

Date:

13-Jan-05 Release date: 02-Aug-05

Protein chain

Q8C863  (ITCH_MOUSE) -  E3 ubiquitin-protein ligase Itchy from Mus musculus

Seq: 864 a.a.

Struc: 37 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.2.3.2.26 - HECT-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: 10.1002/prot.20466

Proteins 60:558-560 (2005)

PubMed id: 15971201

Phosphorylation of either Ser16 or Thr30 does not disrupt the structure of the Itch E3 ubiquitin ligase third WW domain.

A.Z.Shaw, P.Martin-Malpartida, B.Morales, F.Yraola, M.Royo, M.J.Macias.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. a: Itch-ww3 sequence. Two possible sites identified by NetPhos 2.0 phosphorylation prediction server are indicated in red. The immediate amino acid environment of Thr30 is typical of a phosphorylation site for Casein kinase II, CK2, whereas protein kinase A, PKA is predicted to phosphorylate both Thr30 and Ser16. b: A ribbon representation of Itch-ww3 domain showing the side chains of conserved aromatic residues in magenta. Ser16 and Thr30 are displayed in gold. The stereo-view of the best-fit backbone superposition of 10 NMR derived structures selected according to the lowest energy is shown in the Supplementary Material. The structures are displayed with MOLMOL.[20] c: Selected region of 2D NOESY experiments carried out in D[2]O, showing a characteristic pattern of - NOEs found in the WW fold. 1 corresponds to T30-V23, 2 to K12-F22, 3 to N24-W10, and 4 T14-V20. A table containing the proton chemical shifts of the three domains is given as Supplementary Material.

The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 60, 558-560) copyright 2005.