Open AccessStructure of dihydrouridine synthase C (DusC) from Escherichia coli
Author(s) -
Chen Minghao,
Yu Jian,
Tanaka Yoshikazu,
Tanaka Miyuki,
Tanaka Isao,
Yao Min
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113019489
Subject(s) - thermus thermophilus , transfer rna , biology , escherichia coli , atp synthase , stereochemistry , rna , substrate (aquarium) , crystallography , biochemistry , chemistry , enzyme , ecology , gene
Dihydrouridine (D) is one of the most widely conserved tRNA modifications. Dihydrouridine synthase (Dus) is responsible for introducing D modifications into RNA by the reduction of uridine. Recently, a unique substrate‐recognition mechanism using a small adapter molecule has been proposed for Thermus thermophilus Dus ( Tth DusC). To acquire insight regarding its substrate‐recognition mechanism, the crystal structure of DusC from Escherichia coli ( Eco DusC) was determined at 2.1 Å resolution. Eco DusC was shown to be composed of two domains: an N‐terminal catalytic domain and a C‐terminal tRNA‐binding domain. An L‐shaped electron density surrounded by highly conserved residues was found in the active site, as observed for Tth Dus. Structure comparison with Tth Dus indicated that the N‐terminal region has a similar structure, whereas the C‐terminal domain has marked differences in its relative orientation to the N‐terminal domain as well as in its own structure. These observations suggested that Dus proteins adopt a common substrate‐recognition mechanism using an adapter molecule, whereas the manner of tRNA binding is diverse.