4bts | pdb_00004bts

THE CRYSTAL STRUCTURE OF THE EUKARYOTIC 40S RIBOSOMAL SUBUNIT IN COMPLEX WITH EIF1 AND EIF1A

spinqualitylabelsall models 4bts, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bts is a 144 chain structure with sequence from Tetrahymena thermophila and Tetth. This structure supersedes the now removed PDB entries 4bpe, 4bpn, 4bpo and 4bpp. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [I7MK25_TETTS] Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity).[RuleBase:RU004365] [E6PBR9_TETTH] Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits (By similarity).[HAMAP-Rule:MF_03015] Publication Abstract from PubMed Eukaryotic translation initiation factors (eIFs) 1A and 1 are central players in the complex process of start-codon recognition. To improve mechanistic understanding of this process, we determined the crystal structure of the 40S ribosomal subunit in complex with eIF1A and eIF1 from Tetrahymena thermophila at a resolution of 3.7 A. It reveals the positions of the two factors on the 40S and the conformational changes that accompany their binding. The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A.,Weisser M, Voigts-Hoffmann F, Rabl J, Leibundgut M, Ban N Nat Struct Mol Biol. 2013 Jul 14. doi: 10.1038/nsmb.2622. PMID:23851459 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Receptor for activated protein kinase C 1 Ribosome 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA