4v75

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E. coli 70S-fMetVal-tRNAVal-tRNAfMet complex in classic post-translocation state (post1)

Structural highlights

4v75 is a 10 chain structure with sequence from Escherichia coli K-12. This structure supersedes the now removed PDB entries 3j59 and 3j5a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Experimental data:Check to display Experimental Data
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RS15_ECOLI 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 by binding and bridging several RNA helices of the 16S rRNA.[HAMAP-Rule:MF_01343] In the E.coli 70S ribosome it has been modeled (PubMed:12809609) to contact the 23S rRNA of the 50S subunit forming part of bridge B4. In the two 3.5 A resolved ribosome structures (PubMed:16272117) there are minor differences between side-chain conformations.[HAMAP-Rule:MF_01343]

Publication Abstract from PubMed

During protein synthesis, tRNAs move from the ribosome's aminoacyl to peptidyl to exit sites. Here we investigate conformational motions during spontaneous translocation, using molecular dynamics simulations of 13 intermediate-translocation-state models obtained by combining Escherichia coli ribosome crystal structures with cryo-EM data. Resolving fast transitions between states, we find that tRNA motions govern the transition rates within the pre- and post-translocation states. Intersubunit rotations and L1-stalk motion exhibit fast intrinsic submicrosecond dynamics. The L1 stalk drives the tRNA from the peptidyl site and links intersubunit rotation to translocation. Displacement of tRNAs is controlled by 'sliding' and 'stepping' mechanisms involving conserved L16, L5 and L1 residues, thus ensuring binding to the ribosome despite large-scale tRNA movement. Our results complement structural data with a time axis, intrinsic transition rates and molecular forces, revealing correlated functional motions inaccessible by other means.

Energy barriers and driving forces in tRNA translocation through the ribosome.,Bock LV, Blau C, Schroder GF, Davydov II, Fischer N, Stark H, Rodnina MV, Vaiana AC, Grubmuller H Nat Struct Mol Biol. 2013 Nov 3. doi: 10.1038/nsmb.2690. PMID:24186064[1]

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

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See Also

References

  1. ↑ Bock LV, Blau C, Schroder GF, Davydov II, Fischer N, Stark H, Rodnina MV, Vaiana AC, Grubmuller H. Energy barriers and driving forces in tRNA translocation through the ribosome. Nat Struct Mol Biol. 2013 Nov 3. doi: 10.1038/nsmb.2690. PMID:24186064 doi:http://dx.doi.org/10.1038/nsmb.2690

Contents


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4v75, resolution 12.00Å

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