1ucr

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(New page: 200px<br /><applet load="1ucr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ucr, resolution 1.20&Aring;" /> '''Three-dimensional cr...)
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[[Image:1ucr.jpg|left|200px]]<br /><applet load="1ucr" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ucr.jpg|left|200px]]<br /><applet load="1ucr" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ucr, resolution 1.20&Aring;" />
caption="1ucr, resolution 1.20&Aring;" />
'''Three-dimensional crystal structure of dissimilatory sulfite reductase D (DsrD)'''<br />
'''Three-dimensional crystal structure of dissimilatory sulfite reductase D (DsrD)'''<br />
==Overview==
==Overview==
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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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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 Structure==
==About this Structure==
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1UCR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UCR OCA].
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1UCR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UCR OCA].
==Reference==
==Reference==
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[[Category: winged-helix motif]]
[[Category: winged-helix motif]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:01:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:04 2008''

Revision as of 13:23, 21 February 2008


1ucr, resolution 1.20Å

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

Overview

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 Structure

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

Reference

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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