1ucr

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File:1ucr.jpg


1ucr, resolution 1.20Å

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Three-dimensional crystal structure of dissimilatory sulfite reductase D (DsrD)

OverviewOverview

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.

About this StructureAbout this Structure

1UCR is a Single protein structure of sequence from Desulfovibrio vulgaris with SO4 as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of dissimilatory sulfite reductase D (DsrD) protein--possible interaction with B- and Z-DNA by its winged-helix motif., Mizuno N, Voordouw G, Miki K, Sarai A, Higuchi Y, Structure. 2003 Sep;11(9):1133-40. PMID:12962631

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