4v63 | pdb_00004v63

Structural basis for translation termination on the 70S ribosome.

spinqualitylabelsall models 4v63, resolution 3.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4v63 is a 20 chain structure with sequence from Thermus thermophilus HB27. This structure supersedes the now removed PDB entries 3d5a, 3d5b, 3d5c and 3d5d. 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 RS14Z_THET2 Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site (By similarity). Publication Abstract from PubMed At termination of protein synthesis, type I release factors promote hydrolysis of the peptidyl-transfer RNA linkage in response to recognition of a stop codon. Here we describe the crystal structure of the Thermus thermophilus 70S ribosome in complex with the release factor RF1, tRNA and a messenger RNA containing a UAA stop codon, at 3.2 A resolution. The stop codon is recognized in a pocket formed by conserved elements of RF1, including its PxT recognition motif, and 16S ribosomal RNA. The codon and the 30S subunit A site undergo an induced fit that results in stabilization of a conformation of RF1 that promotes its interaction with the peptidyl transferase centre. Unexpectedly, the main-chain amide group of Gln 230 in the universally conserved GGQ motif of the factor is positioned to contribute directly to peptidyl-tRNA hydrolysis. Structural basis for translation termination on the 70S ribosome.,Laurberg M, Asahara H, Korostelev A, Zhu J, Trakhanov S, Noller HF Nature. 2008 Aug 14;454(7206):852-7. Epub 2008 Jul 2. PMID:18596689 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein THX 3D structures Ribosome 3D structures Transfer RNA (tRNA)

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