4U1D

Structure of the PCI domain of translation initiation factor eIF3a

Summary for 4U1D

• Entry DOI: 10.2210/pdb4u1d/pdb
• Descriptor: Eukaryotic translation initiation factor 3 subunit A (1 entity in total)
• Functional Keywords: translation initiation, eif3 complex, pci domain, translation
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Cytoplasm (By similarity): P38249
• Total number of polymer chains: 3
• Total formula weight: 171038.16

Authors

Erzberger, J.P.,Schaefer, T.,Ban, N. (deposition date: 2014-07-15, release date: 2014-09-10, Last modification date: 2024-05-08)

Primary citation

Erzberger, J.P.,Stengel, F.,Pellarin, R.,Zhang, S.,Schaefer, T.,Aylett, C.H.,Cimermancic, P.,Boehringer, D.,Sali, A.,Aebersold, R.,Ban, N.
Molecular Architecture of the 40SeIF1eIF3 Translation Initiation Complex.
Cell, 158:1123-1135, 2014

PubMed 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.

PubMed: 25171412
DOI: 10.1016/j.cell.2014.07.044

Experimental method

X-RAY DIFFRACTION (3.3 Å)