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== | ==The crystal structure of plant sulfite oxidase provides insight into sulfite oxidation in plants and animals== | ||
The molybdenum cofactor (Moco) containing sulfite oxidase (SO) from | <StructureSection load='1ogp' size='340' side='right'caption='[[1ogp]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ogp]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OGP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MTQ:(MOLYBDOPTERIN-S,S)-DIOXO-THIO-MOLYBDENUM(VI)'>MTQ</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=1ogp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ogp OCA], [https://pdbe.org/1ogp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ogp RCSB], [https://www.ebi.ac.uk/pdbsum/1ogp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ogp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SUOX_ARATH SUOX_ARATH] Probably involved in sulfite oxidative detoxification. | |||
== Evolutionary Conservation == | |||
[[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/og/1ogp_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=1ogp ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The molybdenum cofactor (Moco) containing sulfite oxidase (SO) from Arabidopsis thaliana has recently been identified and biochemically characterized. The enzyme is found in peroxisomes and believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution. Plant SO (PSO) is homodimeric and homologous to animal SO, but contains only a single Moco domain without an additional redox center. Here, we present the first crystal structure of a plant Moco enzyme, the apo-state of Arabidopsis SO at 2.6 A resolution. The overall fold and coordination of the Moco are similar to chicken SO (CSO). Comparisons of conserved surface residues and the charge distribution in PSO and CSO reveal major differences near the entrance to both active sites reflecting different electron acceptors. Arg374 has been identified as an important substrate binding residue due to its conformational change when compared to the sulfate bound structure of CSO. | |||
The crystal structure of plant sulfite oxidase provides insights into sulfite oxidation in plants and animals.,Schrader N, Fischer K, Theis K, Mendel RR, Schwarz G, Kisker C Structure. 2003 Oct;11(10):1251-63. PMID:14527393<ref>PMID:14527393</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ogp" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Sulfite Oxidase|Sulfite Oxidase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Fischer K]] | |||
[[Category: Fischer | [[Category: Kisker C]] | ||
[[Category: Kisker | [[Category: Mendel RR]] | ||
[[Category: Mendel | [[Category: Schrader N]] | ||
[[Category: Schrader | [[Category: Schwarz G]] | ||
[[Category: Schwarz | [[Category: Theis K]] | ||
[[Category: Theis | |||
Latest revision as of 15:39, 13 December 2023
The crystal structure of plant sulfite oxidase provides insight into sulfite oxidation in plants and animalsThe crystal structure of plant sulfite oxidase provides insight into sulfite oxidation in plants and animals
Structural highlights
FunctionSUOX_ARATH Probably involved in sulfite oxidative detoxification. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe molybdenum cofactor (Moco) containing sulfite oxidase (SO) from Arabidopsis thaliana has recently been identified and biochemically characterized. The enzyme is found in peroxisomes and believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution. Plant SO (PSO) is homodimeric and homologous to animal SO, but contains only a single Moco domain without an additional redox center. Here, we present the first crystal structure of a plant Moco enzyme, the apo-state of Arabidopsis SO at 2.6 A resolution. The overall fold and coordination of the Moco are similar to chicken SO (CSO). Comparisons of conserved surface residues and the charge distribution in PSO and CSO reveal major differences near the entrance to both active sites reflecting different electron acceptors. Arg374 has been identified as an important substrate binding residue due to its conformational change when compared to the sulfate bound structure of CSO. The crystal structure of plant sulfite oxidase provides insights into sulfite oxidation in plants and animals.,Schrader N, Fischer K, Theis K, Mendel RR, Schwarz G, Kisker C Structure. 2003 Oct;11(10):1251-63. PMID:14527393[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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