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

被引：33

作者：

Mizuno, N

Voordouw, G

Miki, K

Sarai, A

Higuchi, Y

机构：

[1] Himeji Inst Technol, Grad Sch Sci, Dept Life Sci, Kamigori, Hyogo 6781297, Japan

[2] Kyoto Univ, Grad Sch Sci, Div Chem, Kyoto 6068502, Japan

[3] Univ Calgary, Dept Biol Sci, Calgary, AB T2N 1N4, Canada

[4] RIKEN, Tsukuba Inst, Tsukuba, Ibaraki 3050074, Japan

[5] RIKEN, Harima Inst, SPring 8, Mikazuki, Hyogo 6795148, Japan

来源：

STRUCTURE | 2003年 / 11卷 / 09期

关键词：

D O I：

10.1016/S0969-2126(03)00156-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The crystal structure of DsrD from Desulfovibrio vulgraris Hildenborough has been determined at 1.2 Angstrom 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.

引用

页码：1133 / 1140

页数：8