4V67
Crystal structure of a translation termination complex formed with release factor RF2.
This is a non-PDB format compatible entry.
Summary for 4V67
| Entry DOI | 10.2210/pdb4v67/pdb |
| Related | 3D5A 3D5B 3D5C 3D5D |
| Descriptor | 16S RRNA, 30S ribosomal protein S8, 30S ribosomal protein S9, ... (57 entities in total) |
| Functional Keywords | rf2, ribosome, termination, trna |
| Biological source | Thermus thermophilus More |
| Cellular location | Cytoplasm (By similarity): 155076 |
| Total number of polymer chains | 112 |
| Total formula weight | 4621785.47 |
| Authors | Korostelev, A.,Asahara, H.,Lancaster, L.,Laurberg, M.,Hirschi, A.,Noller, H.F. (deposition date: 2008-10-27, release date: 2014-07-09, Last modification date: 2023-09-20) |
| Primary citation | Korostelev, A.,Asahara, H.,Lancaster, L.,Laurberg, M.,Hirschi, A.,Zhu, J.,Trakhanov, S.,Scott, W.G.,Noller, H.F. Crystal structure of a translation termination complex formed with release factor RF2. Proc.Natl.Acad.Sci.USA, 105:19684-19689, 2008 Cited by PubMed Abstract: We report the crystal structure of a translation termination complex formed by the Thermus thermophilus 70S ribosome bound with release factor RF2, in response to a UAA stop codon, solved at 3 A resolution. The backbone of helix alpha5 and the side chain of serine of the conserved SPF motif of RF2 recognize U1 and A2 of the stop codon, respectively. A3 is unstacked from the first 2 bases, contacting Thr-216 and Val-203 of RF2 and stacking on G530 of 16S rRNA. The structure of the RF2 complex supports our previous proposal that conformational changes in the ribosome in response to recognition of the stop codon stabilize rearrangement of the switch loop of the release factor, resulting in docking of the universally conserved GGQ motif in the PTC of the 50S subunit. As seen for the RF1 complex, the main-chain amide nitrogen of glutamine in the GGQ motif is positioned to contribute directly to catalysis of peptidyl-tRNA hydrolysis, consistent with mutational studies, which show that most side-chain substitutions of the conserved glutamine have little effect. We show that when the H-bonding capability of the main-chain N-H of the conserved glutamine is eliminated by substitution with proline, peptidyl-tRNA esterase activity is abolished, consistent with its proposed role in catalysis. PubMed: 19064930DOI: 10.1073/pnas.0810953105 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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