3W9Z

Crystal structure of DusC

Summary for 3W9Z

• Entry DOI: 10.2210/pdb3w9z/pdb
• Related: 1VHN 3B0P 3B0U 3B0V
• Descriptor: tRNA-dihydrouridine synthase C, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: tim barrel, reductase, trna, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 36654.76

Authors

Chen, M.,Yu, J.,Tanaka, Y.,Tanaka, I.,Yao, M. (deposition date: 2013-04-19, release date: 2013-07-31, Last modification date: 2024-03-20)

Primary citation

Chen, M.,Yu, J.,Tanaka, Y.,Tanaka, M.,Tanaka, I.,Yao, M.
Structure of dihydrouridine synthase C (DusC) from Escherichia coli
Acta Crystallogr.,Sect.F, 69:834-838, 2013

PubMed Abstract: 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 (TthDusC). To acquire insight regarding its substrate-recognition mechanism, the crystal structure of DusC from Escherichia coli (EcoDusC) was determined at 2.1 Å resolution. EcoDusC 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 TthDus. Structure comparison with TthDus 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.

PubMed: 23908023
DOI: 10.1107/S1744309113019489

Experimental method

X-RAY DIFFRACTION (2.1 Å)