5ZTB

Structure of Sulfurtransferase

Summary for 5ZTB

• Entry DOI: 10.2210/pdb5ztb/pdb
• Descriptor: Sulfur carrier protein TtuB, tRNA-5-methyluridine(54) 2-sulfurtransferase, GLYCEROL, ... (8 entities in total)
• Functional Keywords: sulfur transfer, iron-sulfur cluster, trna binding protein, complex, rna binding protein, rna binding protein-transferase complex, rna binding protein/transferase
• Biological source: Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039); More
• Total number of polymer chains: 6
• Total formula weight: 137628.44

Authors

Tanaka, Y.,Chen, M.,Narai, S.,Yao, M. (deposition date: 2018-05-02, release date: 2019-06-12, Last modification date: 2024-03-27)

Primary citation

Chen, M.,Ishizaka, M.,Narai, S.,Horitani, M.,Shigi, N.,Yao, M.,Tanaka, Y.
The [4Fe-4S] cluster of sulfurtransferase TtuA desulfurizes TtuB during tRNA modification in Thermus thermophilus.
Commun Biol, 3:168-168, 2020

PubMed Abstract: TtuA and TtuB are the sulfurtransferase and sulfur donor proteins, respectively, for biosynthesis of 2-thioribothymidine (sT) at position 54 of transfer RNA (tRNA), which is responsible for adaptation to high temperature environments in Thermus thermophilus. The enzymatic activity of TtuA requires an iron-sulfur (Fe-S) cluster, by which a sulfur atom supplied by TtuB is transferred to the tRNA substrate. Here, we demonstrate that the Fe-S cluster directly receives sulfur from TtuB through its inherent coordination ability. TtuB forms a [4Fe-4S]-TtuB intermediate, but that sulfur is not immediately released from TtuB. Further desulfurization assays and mutation studies demonstrated that the release of sulfur from the thiocarboxylated C-terminus of TtuB is dependent on adenylation of the substrate tRNA, and the essential residue for TtuB desulfurization was identified. Based on these findings, the molecular mechanism of sulfur transfer from TtuB to Fe-S cluster is proposed.

PubMed: 32265486
DOI: 10.1038/s42003-020-0895-3

Experimental method

X-RAY DIFFRACTION (2.2 Å)