Structural highlights
Function
[THTR_YEAST] Required for formation of the 2-thio group of the 5-methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs.[1]
Publication Abstract from PubMed
Yeast tRNA-thiouridine modification protein 1 (Tum1) plays essential role in the sulfur transfer process of Urm1 system, which in turn is involved in many important cellular processes. In the rhodanese-like domain (RLD), conserved cysteine residue is proved to be the centre of active site of sulfurtransferases and crucial for the substrate recognition. In this report, we describe the crystal structure of Tum1 protein at 1.90 A resolution which, despite consisting of two RLDs, has only one conserved cysteine residue in the C-terminal RLD. An unaccounted electron density is found near the active site, which might point to the new cofactor in the sulfur transfer mechanism.
Crystal structure of the Tum1 protein from the yeast Saccharomyces cerevisiae.,Qiu R, Wang F, Liu M, Lou T, Ji C Protein Pept Lett. 2012 May 8. PMID:22587783[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Huang B, Lu J, Bystrom AS. A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae. RNA. 2008 Oct;14(10):2183-94. doi: 10.1261/rna.1184108. Epub 2008 Aug 28. PMID:18755837 doi:10.1261/rna.1184108
- ↑ Qiu R, Wang F, Liu M, Lou T, Ji C. Crystal structure of the Tum1 protein from the yeast Saccharomyces cerevisiae. Protein Pept Lett. 2012 May 8. PMID:22587783
