Structural highlights
4y4o is a 20 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 2.3Å |
| Ligands: | 0TD, 2MA, 2MG, 2MU, 4OC, 5MC, 5MU, 7MG, ARG, M2G, MA6, MG, MPD, OMG, PSU, SF4, UR3, ZN |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
RL2_THET8 One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial (By similarity). Makes several contacts with the 16S rRNA (forming bridge B7b) in the 70S ribosome.[HAMAP-Rule:MF_01320_B]
Publication Abstract from PubMed
We report crystal structures of the Thermus thermophilus ribosome at 2.3- to 2.5-A resolution, which have enabled modeling of rRNA modifications. The structures reveal contacts of modified nucleotides with mRNA and tRNAs or protein pY, and contacts within the ribosome interior stabilizing the functional fold of rRNA. Our work provides a resource to explore the roles of rRNA modifications and yields a more comprehensive atomic model of a bacterial ribosome.
Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly.,Polikanov YS, Melnikov SV, Soll D, Steitz TA Nat Struct Mol Biol. 2015 Apr;22(4):342-4. doi: 10.1038/nsmb.2992. Epub 2015 Mar , 16. PMID:25775268[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Polikanov YS, Melnikov SV, Soll D, Steitz TA. Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly. Nat Struct Mol Biol. 2015 Apr;22(4):342-4. doi: 10.1038/nsmb.2992. Epub 2015 Mar , 16. PMID:25775268 doi:https://dx.doi.org/10.1038/nsmb.2992
