| Structural highlights
2uub is a 23 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| Ligands: | , , , |
NonStd Res: | , |
Related: | 1fjg, 1gix, 1i94, 1i95, 1i96, 1i97, 1ibk, 1ibl, 1ibm, 1j5e, 1jgo, 1jgp, 1jgq, 1l1u, 1n32, 1n33, 1n34, 1n36, 1pns, 1pnx, 1xmo, 1xmq, 1xnq, 1xnr, 1yl4, 2b64, 2b9m, 2b9o, 2f4v, 2j00, 2j02, 2uu9, 2uua, 2uuc, 1fka, 1hnw, 1hnx, 1hnz, 1hr0, 1qd7, 1twt, 1g1x, 1dv4, 1eg0, 1rss, 1emi, 1mvr, 1pn7, 1pn8, 1qzc |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[RS16_THET8] Binds to the lower part of the body of the 30S subunit, where it stabilizes two of its domains.[HAMAP-Rule:MF_00385] [RS6_THET8] Located on the outer edge of the platform on the body of the 30S subunit.[HAMAP-Rule:MF_00360] [RS9_THET8] Part of the top of the head of the 30S subunit. The C-terminal region penetrates the head emerging in the P-site where it contacts tRNA.[HAMAP-Rule:MF_00532_B] [RS8_THET8] One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit central domain. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.[HAMAP-Rule:MF_01302_B]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Mechanism for expanding the decoding capacity of transfer RNAs by modification of uridines.,Weixlbaumer A, Murphy FV 4th, Dziergowska A, Malkiewicz A, Vendeix FA, Agris PF, Ramakrishnan V Nat Struct Mol Biol. 2007 Jun;14(6):498-502. Epub 2007 May 13. PMID:17496902[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weixlbaumer A, Murphy FV 4th, Dziergowska A, Malkiewicz A, Vendeix FA, Agris PF, Ramakrishnan V. Mechanism for expanding the decoding capacity of transfer RNAs by modification of uridines. Nat Struct Mol Biol. 2007 Jun;14(6):498-502. Epub 2007 May 13. PMID:17496902 doi:10.1038/nsmb1242
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