2q62

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Current revision (09:14, 21 February 2024) (edit) (undo)
 
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<StructureSection load='2q62' size='340' side='right'caption='[[2q62]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2q62' size='340' side='right'caption='[[2q62]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2q62]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_9930 Atcc 9930]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q62 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2q62]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q62 FirstGlance]. <br>
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</td></tr><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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">arsH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=382 ATCC 9930])</td></tr>
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<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=2q62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q62 OCA], [https://pdbe.org/2q62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q62 RCSB], [https://www.ebi.ac.uk/pdbsum/2q62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q62 ProSAT]</span></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=2q62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q62 OCA], [https://pdbe.org/2q62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q62 RCSB], [https://www.ebi.ac.uk/pdbsum/2q62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q62 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ARREH_RHIME ARREH_RHIME] Has NADPH-dependent FMN reductase activity. No activity with NADH. May play a role in resistance to heavy metal toxicity.<ref>PMID:17673204</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2q62 ConSurf].
</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=2q62 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Purified ArsH from Sinorhizobium meliloti exhibits NADPH:FMN-dependent reduction of molecular O2 to hydrogen peroxide and catalyzes reduction of azo dyes. The structure of ArsH was determined at 1.8A resolution. ArsH crystallizes with eight molecules in the asymmetric unit forming two tetramers. Each monomer has a core domain with a central five-stranded parallel beta-sheet and two monomers interact to form a classical flavodoxin-like dimer. The N- and C-terminal extensions of ArsH are involved in interactions between subunits and tetramer formation. The structure may provide insight in how ArsH participates in arsenic detoxification.
 
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Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti.,Ye J, Yang HC, Rosen BP, Bhattacharjee H FEBS Lett. 2007 Aug 21;581(21):3996-4000. Epub 2007 Jul 25. PMID:17673204<ref>PMID:17673204</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2q62" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 9930]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bhattacharjee, H]]
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[[Category: Sinorhizobium meliloti]]
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[[Category: Rosen, B P]]
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[[Category: Bhattacharjee H]]
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[[Category: Yang, H]]
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[[Category: Rosen BP]]
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[[Category: Ye, J]]
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[[Category: Yang H]]
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[[Category: Alpha/beta]]
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[[Category: Ye J]]
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[[Category: Flavoprotein]]
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Current revision

Crystal Structure of ArsH from Sinorhizobium meliloti

PDB ID 2q62

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