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Translation initiation factor eIF3b contains a nine-bladed β-propeller and interacts with the 40S ribosomal subunit.
- Source :
-
Structure (London, England : 1993) [Structure] 2014 Jun 10; Vol. 22 (6), pp. 923-30. Date of Electronic Publication: 2014 Apr 24. - Publication Year :
- 2014
-
Abstract
- The multisubunit eukaryotic translation initiation factor 3, among which the subunit b (eIF3b) is a major scaffold protein, plays essential roles in protein synthesis. Here, we report the crystal structure of the WD40 domain of Chaetomium thermophilum eIF3b, revealing a nine-bladed β-propeller fold. Sequence analysis indicates that this propeller architecture is common to all eIF3b orthologs. Revisiting the cryoelectron microscopy (cryo-EM) map of the 43S preinitiation complex suggests an interaction of the eIF3b with the 40S ribosomal subunit involving the ribosomal protein S9e and the 18S rRNA. This model is strongly supported by the direct binding of eIF3b to 40S ribosomes and to the isolated ribosomal protein rpS9e in vitro.<br /> (Copyright © 2014 Elsevier Ltd. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Binding Sites
Chaetomium chemistry
Chaetomium genetics
Conserved Sequence
Crystallography, X-Ray
Eukaryotic Initiation Factor-3 genetics
Fungal Proteins genetics
Models, Molecular
Protein Conformation
Protein Folding
Protein Interaction Domains and Motifs
Protein Subunits
Sequence Homology, Amino Acid
Eukaryotic Initiation Factor-3 chemistry
Fungal Proteins chemistry
Ribosome Subunits, Small, Eukaryotic chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1878-4186
- Volume :
- 22
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Structure (London, England : 1993)
- Publication Type :
- Academic Journal
- Accession number :
- 24768115
- Full Text :
- https://doi.org/10.1016/j.str.2014.03.010