1ucr: Difference between revisions

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[[Image:1ucr.jpg|left|200px]]


{{Structure
==Three-dimensional crystal structure of dissimilatory sulfite reductase D (DsrD)==
|PDB= 1ucr |SIZE=350|CAPTION= <scene name='initialview01'>1ucr</scene>, resolution 1.20&Aring;
<StructureSection load='1ucr' size='340' side='right'caption='[[1ucr]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
<table><tr><td colspan='2'>[[1ucr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UCR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UCR FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ucr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ucr OCA], [https://pdbe.org/1ucr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ucr RCSB], [https://www.ebi.ac.uk/pdbsum/1ucr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ucr ProSAT]</span></td></tr>
 
</table>
'''Three-dimensional crystal structure of dissimilatory sulfite reductase D (DsrD)'''
== Function ==
 
[https://www.uniprot.org/uniprot/DSVD_DESVH DSVD_DESVH] May play an essential role in dissimilatory sulfite reduction.
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uc/1ucr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ucr ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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==
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<ref>PMID:12962631</ref>
1UCR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UCR OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://www.ncbi.nlm.nih.gov/pubmed/12962631 12962631]
</div>
<div class="pdbe-citations 1ucr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Desulfovibrio vulgaris]]
[[Category: Desulfovibrio vulgaris]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Higuchi, Y.]]
[[Category: Higuchi Y]]
[[Category: Miki, K.]]
[[Category: Miki K]]
[[Category: Mizuno, N.]]
[[Category: Mizuno N]]
[[Category: Sarai, A.]]
[[Category: Sarai A]]
[[Category: Voordouw, G.]]
[[Category: Voordouw G]]
[[Category: SO4]]
[[Category: crystal structure]]
[[Category: dissimilatory sulfite reductase d]]
[[Category: dna binding motif]]
[[Category: sulfate-reducing bacteria]]
[[Category: winged-helix motif]]
 
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