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Article

Crystallographic study of the 2-thioribothymidine-synthetic complex TtuA-TtuB from Thermus thermophilus.

Acta crystallographica. Section F, Structural biology communications - 1 Oct 2016

Chen Minghao, Narai Shun, Omura Naoki, Shigi Naoki, Chimnaronk Sarin, Tanaka Yoshikazu, Yao Min

Abstract excerpt

The ubiquitin-like protein TtuB is a sulfur carrier for the biosynthesis of 2-thioribothymidine (s2T) at position 54 in some thermophilic bacterial tRNAs. TtuB captures a S atom at its C-terminus as a thiocarboxylate and transfers it to tRNA by the transferase activity of TtuA. TtuB also functions to suppress s2T formation by forming a covalent bond with TtuA. To explore how TtuB interacts with TtuA and switches...

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Identifiers

PMID: 27710943
DOI: 10.1107/S2053230X16014242
PMCID: PMC5053163

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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