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Article

Structural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling.

Nature communications - 9 Sept 2021

van der Stel Anne-Xander, Gordon Emily R, Sengupta Arnab, Martínez Allyson K, Klepacki Dorota, Perry Thomas N, Herrero Del Valle Alba, Vázquez-Laslop Nora, Sachs Matthew S, Cruz-Vera Luis R, Innis C Axel

Abstract excerpt

Free L-tryptophan (L-Trp) stalls ribosomes engaged in the synthesis of TnaC, a leader peptide controlling the expression of the Escherichia coli tryptophanase operon. Despite extensive characterization, the molecular mechanism underlying the recognition and response to L-Trp by the TnaC-ribosome complex remains unknown. Here, we use a combined biochemical and structural approach to characterize a TnaC variant...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 34504068
DOI: 10.1038/s41467-021-25663-8
PMCID: PMC8429421

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structural basis for the tryptophan sensitivity of TnaC-mediated ribosome stalling.PMID 34504068Read ↗

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