PDBsum entry 6fbz

Translation

PDB id: 6fbz

Contents

Protein chains

191 a.a.

78 a.a.

Ligands

MGP

Waters ×134

PDB id:

6fbz

Name:

Translation

Title:

Crystal structure of the eif4e-eif4g complex from chaetomium thermophilum in the cap-bound state

Structure:

Eukaryotic translation initiation factor 4e-like protein, eukaryotic translation initiation factor 4e-like protein. Chain: a. Engineered: yes. Eukaryotic translation initiation factor 4g. Chain: b. Engineered: yes

Source:

Chaetomium thermophilum var. Thermophilum dsm 1495. Organism_taxid: 759272. Gene: ctht_0058450. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: ctht_0071550. Expression_system_taxid: 469008

Resolution:

1.50Å R-factor: 0.172 R-free: 0.206

Authors:

S.Gruener,E.Valkov

Key ref:

S.Grüner et al. (2018). Structural motifs in eIF4G and 4E-BPs modulate their binding to eIF4E to regulate translation initiation in yeast. Nucleic Acids Res, 46, 6893-6908. PubMed id: 30053226

Date:

20-Dec-17 Release date: 27-Jun-18

Protein chain

G0SCU4  (G0SCU4_CHATD) -  Eukaryotic translation initiation factor 4E-like protein from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

Seq: 250 a.a.

Struc: 191 a.a.*

Protein chain

G0SFP0  (G0SFP0_CHATD) -  MIF4G domain-containing protein from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

Seq: 1608 a.a.

Struc: 78 a.a.*

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

Nucleic Acids Res 46:6893-6908 (2018)

PubMed id: 30053226

Structural motifs in eIF4G and 4E-BPs modulate their binding to eIF4E to regulate translation initiation in yeast.

S.Grüner, R.Weber, D.Peter, M.Y.Chung, C.Igreja, E.Valkov, E.Izaurralde.

ABSTRACT

The interaction of the eukaryotic initiation factor 4G (eIF4G) with the cap-binding protein eIF4E initiates cap-dependent translation and is regulated by the 4E-binding proteins (4E-BPs), which compete with eIF4G to repress translation. Metazoan eIF4G and 4E-BPs interact with eIF4E via canonical and non-canonical motifs that bind to the dorsal and lateral surface of eIF4E in a bipartite recognition mode. However, previous studies pointed to mechanistic differences in how fungi and metazoans regulate protein synthesis. We present crystal structures of the yeast eIF4E bound to two yeast 4E-BPs, p20 and Eap1p, as well as crystal structures of a fungal eIF4E-eIF4G complex. We demonstrate that the core principles of molecular recognition of eIF4E are in fact highly conserved among translational activators and repressors in eukaryotes. Finally, we reveal that highly specialized structural motifs do exist and serve to modulate the affinity of protein-protein interactions that regulate cap-dependent translation initiation in fungi.