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Crystal structure of dissimilatory sulfite reductase D (DsrD) protein--possible interaction with B- and Z-DNA by its winged-helix motif.

Authors
  • Mizuno, Nobuhiro
  • Voordouw, Gerrit
  • Miki, Kunio
  • Sarai, Akinori
  • Higuchi, Yoshiki
Type
Published Article
Journal
Structure
Publisher
Elsevier BV
Publication Date
Sep 01, 2003
Volume
11
Issue
9
Pages
1133–1140
Identifiers
PMID: 12962631
Source
Medline
License
Unknown

Abstract

The crystal structure of DsrD from Desulfovibrio vulgaris Hildenborough has been determined at 1.2 A resolution. DsrD is in a dimeric form in the crystal, and five sulfate anions were located on the surface. The structure of DsrD comprises a winged-helix motif, which shows the highest structural homology to similar motifs found in Z-DNA binding proteins and some B-DNA binding proteins. The core structure of the molecule is constructed by intramolecular interactions of hydrophobic residues, which are well conserved in DNA binding proteins, suggesting that these proteins belong to the same superfamily on the basis of the structure. These results indicate a possible role of DsrD in transcription or translation of genes for enzymes catalyzing dissimilatory sulfite reduction.

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