1ogp: Difference between revisions

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-{{Seed}}
-[[Image:1ogp.png|left|200px]]
-<!--
+==The crystal structure of plant sulfite oxidase provides insight into sulfite oxidation in plants and animals==
-The line below this paragraph, containing "STRUCTURE_1ogp", creates the "Structure Box" on the page.
+<StructureSection load='1ogp' size='340' side='right'caption='[[1ogp]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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>
-{{STRUCTURE_1ogp|  PDB=1ogp  |  SCENE=  }}
+<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 INSIGHT INTO SULFITE OXIDATION IN PLANTS AND ANIMALS===
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1ogp" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_14527393}}, adds the Publication Abstract to the page
+*[[Sulfite Oxidase|Sulfite Oxidase]]
-(as it appears on PubMed at http://www.pubmed.gov), where 14527393 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_14527393}}
+__TOC__
+</StructureSection>
-==About this Structure==
-OGP is a [[Single protein]] structure of sequence from [http://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].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/14527393 14527393]
 [[Category: Arabidopsis thaliana]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Sulfite oxidase]]
+[[Category: Fischer K]]
-[[Category: Fischer, K.]]
+[[Category: Kisker C]]
-[[Category: Kisker, C.]]
+[[Category: Mendel RR]]
-[[Category: Mendel, R R.]]
+[[Category: Schrader N]]
-[[Category: Schrader, N.]]
+[[Category: Schwarz G]]
-[[Category: Schwarz, G.]]
+[[Category: Theis K]]
-[[Category: Theis, K.]]
-[[Category: Intramolecular electron transfer,oxidoreducta]]
-[[Category: Molybdenum cofactor]]
-[[Category: Molybdopterin]]
-[[Category: Peroxisome]]
-[[Category: Plant sulfite oxidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:15:19 2008''