PDBsum entry 2mbh

Transcription

PDB id: 2mbh

Contents

Protein chains

19 a.a.

76 a.a.

PDB id:

2mbh

Name:

Transcription

Title:

Nmr structure of eklf(22-40)/ubiquitin complex

Structure:

Krueppel-like factor 1. Chain: b. Synonym: erythroid krueppel-like transcription factor, eklf. Engineered: yes. Ubiquitin. Chain: a. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: klf1, eklf. Expressed in: escherichia coli. Expression_system_taxid: 562. Rainbow trout. Gene: ubb.

NMR struc:

20 models

Authors:

L.Raiola,J.G.Omichinski

Key ref:

L.Raiola et al. (2013). Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. Structure, 21, 2014-2024. PubMed id: 24139988 DOI: 10.1016/j.str.2013.08.027

Date:

31-Jul-13 Release date: 09-Oct-13

Protein chain

Q13351  (KLF1_HUMAN) -  Krueppel-like factor 1 from Homo sapiens

Seq: 362 a.a.

Struc: 19 a.a.

Protein chain

P62987  (RL40_HUMAN) -  Ubiquitin-ribosomal protein eL40 fusion protein from Homo sapiens

Seq: 128 a.a.

Struc: 76 a.a.

Enzyme reactions

• Enzyme class: Chains B, A: E.C.?

DOI no: 10.1016/j.str.2013.08.027

Structure 21:2014-2024 (2013)

PubMed id: 24139988

Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF.

L.Raiola, M.Lussier-Price, D.Gagnon, J.Lafrance-Vanasse, X.Mascle, G.Arseneault, P.Legault, J.Archambault, J.G.Omichinski.

ABSTRACT

Like other acidic transactivation domains (TAD), the minimal TAD from the erythroid-specific transcription factor EKLF (EKLFTAD) has been shown to contribute both to its transcriptional activity as well as to its ubiquitin(UBI)-mediated degradation. In this article, we examine the activation-degradation role of the acidic TAD of EKLF and demonstrate that the first 40 residues (EKLFTAD1) within this region form a noncovalent interaction with UBI. Nuclear magnetic resonance (NMR) structural studies of an EKLFTAD1-UBI complex show that EKLFTAD1 adopts a 14-residue α helix that forms the recognition interface with UBI in a similar manner as the UBI-interacting helix of Rabex5. We also identify a similar interaction between UBI and the activation-degradation region of SREBP1a, but not with the activation-degradation regions of p53, GAL4, and VP16. These results suggest that select activation-degradation regions like the ones found in EKLF and SREBP1a function in part through their ability to form noncovalent interactions with UBI.