3utn

Crystal structure of Tum1 protein from Saccharomyces cerevisiae

spinqualitylabelsall models 3utn, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3utn is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: DMS, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function THTR_YEAST Required for formation of the 2-thio group of the 5-methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sulfurtransferase

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