4v5e

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Insights into translational termination from the structure of RF2 bound to the ribosomeInsights into translational termination from the structure of RF2 bound to the ribosome

Structural highlights

4v5e is a 20 chain structure with sequence from Thermus thermophilus HB8. This structure supersedes the now removed PDB entries 2wh1, 2wh2, 2wh3, 2wh4, 2jl5, 2jl6, 2jl7 and 2jl8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.45Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RS5_THET8 With S4 and S12 plays an important role in translational accuracy (By similarity).[HAMAP-Rule:MF_01307_B] Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Binds mRNA in the 70S ribosome, positioning it for translation.[HAMAP-Rule:MF_01307_B]

Publication Abstract from PubMed

The termination of protein synthesis occurs through the specific recognition of a stop codon in the A site of the ribosome by a release factor (RF), which then catalyzes the hydrolysis of the nascent protein chain from the P-site transfer RNA. Here we present, at a resolution of 3.5 angstroms, the crystal structure of RF2 in complex with its cognate UGA stop codon in the 70S ribosome. The structure provides insight into how RF2 specifically recognizes the stop codon; it also suggests a model for the role of a universally conserved GGQ motif in the catalysis of peptide release.

Insights into translational termination from the structure of RF2 bound to the ribosome.,Weixlbaumer A, Jin H, Neubauer C, Voorhees RM, Petry S, Kelley AC, Ramakrishnan V Science. 2008 Nov 7;322(5903):953-6. PMID:18988853[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Weixlbaumer A, Jin H, Neubauer C, Voorhees RM, Petry S, Kelley AC, Ramakrishnan V. Insights into translational termination from the structure of RF2 bound to the ribosome. Science. 2008 Nov 7;322(5903):953-6. PMID:18988853 doi:http://dx.doi.org/322/5903/953

4v5e, resolution 3.45Å

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OCA