2UUA
Structure of the Thermus thermophilus 30S ribosomal subunit complexed with a Valine-ASL with cmo5U in position 34 bound to an mRNA with a GUC-codon in the A-site and paromomycin.
Summary for 2UUA
| Entry DOI | 10.2210/pdb2uua/pdb |
| Related | 1FJG 1GIX 1HNW 1HNX 1HNZ 1HR0 1I94 1I95 1I96 1I97 1IBK 1IBL 1IBM 1J5E 1JGO 1JGP 1JGQ 1L1U 1N32 1N33 1N34 1N36 1PNS 1PNX 1XMO 1XMQ 1XNQ 1XNR 1YL4 2J00 2J02 2UU9 2UUB 2UUC |
| Descriptor | 16S RRNA, 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (27 entities in total) |
| Functional Keywords | trna-binding, rrna-binding, metal-binding, zinc-finger, translation, coiled coil, paromomycin, trna, zinc, mrna, cmo5u, ribosome, rna-binding, modifiactions, ribosomal protein, ribonucleoprotein |
| Biological source | THERMUS THERMOPHILUS More |
| Total number of polymer chains | 23 |
| Total formula weight | 796806.00 |
| Authors | Weixlbaumer, A.,Murphy, F.V.,Dziergowska, A.,Malkiewicz, A.,Vendeix, F.A.P.,Agris, P.F.,Ramakrishnan, V. (deposition date: 2007-03-01, release date: 2007-05-15, Last modification date: 2023-12-13) |
| Primary citation | Weixlbaumer, A.,Murphy 4th., F.V.,Dziergowska, A.,Malkiewicz, A.,Vendeix, F.A.,Agris, P.F.,Ramakrishnan, V. Mechanism for expanding the decoding capacity of transfer RNAs by modification of uridines. Nat. Struct. Mol. Biol., 14:498-502, 2007 Cited by PubMed Abstract: One of the most prevalent base modifications involved in decoding is uridine 5-oxyacetic acid at the wobble position of tRNA. It has been known for several decades that this modification enables a single tRNA to decode all four codons in a degenerate codon box. We have determined structures of an anticodon stem-loop of tRNA(Val) containing the modified uridine with all four valine codons in the decoding site of the 30S ribosomal subunit. An intramolecular hydrogen bond involving the modification helps to prestructure the anticodon loop. We found unusual base pairs with the three noncomplementary codon bases, including a G.U base pair in standard Watson-Crick geometry, which presumably involves an enol form for the uridine. These structures suggest how a modification in the uridine at the wobble position can expand the decoding capability of a tRNA. PubMed: 17496902DOI: 10.1038/nsmb1242 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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