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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Crystal Structure of the Tum1 Protein from the Yeast Saccharomyces cerevisiae

Author(s): Rui Qiu, Fengbin Wang, Meiruo Liu, Tiantian Lou and Chaoneng Ji

Volume 19, Issue 11, 2012

Page: [1139 - 1143] Pages: 5

DOI: 10.2174/092986612803217060

Price: $65

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 Å 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.

Keywords: 3-mercaptopyruvate sulfurtransferase, rhodanese, Saccharomyces cerevisiae, tum1, tRNA-thiouridine modification protein, ubiquitin-related modifier


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