3UTN

Crystal structure of Tum1 protein from Saccharomyces cerevisiae

Summary for 3UTN

• Entry DOI: 10.2210/pdb3utn/pdb
• Descriptor: Thiosulfate sulfurtransferase TUM1, DIMETHYL SULFOXIDE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: rhodanese-like domain, sulfurtransferase, transferase
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 37520.87

Authors

Qiu, R.,Wang, F.,Liu, M.,Ji, C.,Gong, W. (deposition date: 2011-11-26, release date: 2012-10-17, Last modification date: 2023-11-08)

Primary citation

Qiu, R.,Wang, F.,Liu, M.,Lou, T.,Ji, C.
Crystal structure of the Tum1 protein from the yeast Saccharomyces cerevisiae.
Protein Pept.Lett., 19:1139-1143, 2012

PubMed Abstract: 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.

PubMed: 22587783
DOI: 10.2174/092986612803217060

Experimental method

X-RAY DIFFRACTION (1.9 Å)