PDBsum entry 4u1c

Translation

PDB id: 4u1c

Contents

Protein chains

544 a.a.

271 a.a.

PDB id:

4u1c

Name:

Translation

Title:

Crystal structure of the eif3a/eif3c pci-domain heterodimer

Structure:

Eukaryotic translation initiation factor 3 subunit c. Chain: c. Synonym: eif3c,eukaryotic translation initiation factor 3 93 kda subunit,eif3 p93,nuclear transport protein nip1,translation initiation factor eif3,p93 subunit. Engineered: yes. Eukaryotic translation initiation factor 3 subunit a. Chain: a. Synonym: eif3a,eukaryotic translation initiation factor 3 110 kda

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: nip1, ymr309c, ym9924.01c, ym9952.11c. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: rpg1, tif32, ybr079c, ybr0734.

Resolution:

3.50Å R-factor: 0.264 R-free: 0.293

Authors:

J.P.Erzberger,T.Schaefer,N.Ban

Key ref:

J.P.Erzberger et al. (2014). Molecular architecture of the 40S⋅eIF1⋅eIF3 translation initiation complex. Cell, 158, 1123-1135. PubMed id: 25171412 DOI: 10.1016/j.cell.2014.07.044

Date:

15-Jul-14 Release date: 10-Sep-14

Protein chain

P32497  (EIF3C_YEAST) -  Eukaryotic translation initiation factor 3 subunit C from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 812 a.a.

Struc: 544 a.a.

Protein chain

P38249  (EIF3A_YEAST) -  Eukaryotic translation initiation factor 3 subunit A from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 964 a.a.

Struc: 271 a.a.

DOI no: 10.1016/j.cell.2014.07.044

Cell 158:1123-1135 (2014)

PubMed id: 25171412

Molecular architecture of the 40S⋅eIF1⋅eIF3 translation initiation complex.

J.P.Erzberger, F.Stengel, R.Pellarin, S.Zhang, T.Schaefer, C.H.Aylett, P.Cimermančič, D.Boehringer, A.Sali, R.Aebersold, N.Ban.

ABSTRACT

Eukaryotic translation initiation requires the recruitment of the large, multiprotein eIF3 complex to the 40S ribosomal subunit. We present X-ray structures of all major components of the minimal, six-subunit Saccharomyces cerevisiae eIF3 core. These structures, together with electron microscopy reconstructions, cross-linking coupled to mass spectrometry, and integrative structure modeling, allowed us to position and orient all eIF3 components on the 40S⋅eIF1 complex, revealing an extended, modular arrangement of eIF3 subunits. Yeast eIF3 engages 40S in a clamp-like manner, fully encircling 40S to position key initiation factors on opposite ends of the mRNA channel, providing a platform for the recruitment, assembly, and regulation of the translation initiation machinery. The structures of eIF3 components reported here also have implications for understanding the architecture of the mammalian 43S preinitiation complex and the complex of eIF3, 40S, and the hepatitis C internal ribosomal entry site RNA.