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TitleMolecular basis for the ribosome functioning as an L-tryptophan sensor.
Journal, issue, pagesCell Rep, Vol. 9, Issue 2, Page 469-475, Year 2014
Publish dateOct 23, 2014
AuthorsLukas Bischoff / Otto Berninghausen / Roland Beckmann /
PubMed AbstractElevated levels of the free amino acid L-tryptophan (L-Trp) trigger expression of the tryptophanase tnaCAB operon in E. coli. Activation depends on tryptophan-dependent ribosomal stalling during ...Elevated levels of the free amino acid L-tryptophan (L-Trp) trigger expression of the tryptophanase tnaCAB operon in E. coli. Activation depends on tryptophan-dependent ribosomal stalling during translation of the upstream TnaC peptide. Here, we present a cryoelectron microscopy (cryo-EM) reconstruction at 3.8 Å resolution of a ribosome stalled by the TnaC peptide. Unexpectedly, we observe two L-Trp molecules in the ribosomal exit tunnel coordinated within composite hydrophobic pockets formed by the nascent TnaC peptide and the tunnel wall. As a result, the peptidyl transferase center (PTC) adopts a distinct conformation that precludes productive accommodation of release factor 2 (RF2), thereby inducing translational stalling. Collectively, our results demonstrate how the translating ribosome can act as a small molecule sensor for gene regulation.
External linksCell Rep / PubMed:25310980
MethodsEM (single particle)
Resolution3.8 Å
Structure data

2773

4uy8

EMDB-2773, PDB-4uy8:
Molecular basis for the ribosome functioning as a L-tryptophan sensor - Cryo-EM structure of a TnaC stalled E.coli ribosome
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-TRP:
TRYPTOPHAN

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsRIBOSOME / TNAC / TRANSLATION REGULATION

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