Structural highlights
Function
G0RXS6_CHATD Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome (By similarity).[PIRNR:PIRNR036424][HAMAP-Rule:MF_03001]
Publication Abstract from PubMed
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 beta-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.
Translation initiation factor eIF3b contains a nine-bladed beta-propeller and interacts with the 40S ribosomal subunit.,Liu Y, Neumann P, Kuhle B, Monecke T, Schell S, Chari A, Ficner R Structure. 2014 Jun 10;22(6):923-30. doi: 10.1016/j.str.2014.03.010. Epub 2014, Apr 24. PMID:24768115[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu Y, Neumann P, Kuhle B, Monecke T, Schell S, Chari A, Ficner R. Translation initiation factor eIF3b contains a nine-bladed beta-propeller and interacts with the 40S ribosomal subunit. Structure. 2014 Jun 10;22(6):923-30. doi: 10.1016/j.str.2014.03.010. Epub 2014, Apr 24. PMID:24768115 doi:http://dx.doi.org/10.1016/j.str.2014.03.010
