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==CRYSTAL STRUCTURE OF RUBISCO FROM CHLAMYDOMONAS REINHARDTII WITH A LARGE-SUBUNIT V331A MUTATION==
 
<StructureSection load='2v63' size='340' side='right' caption='[[2v63]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
==Crystal structure of Rubisco from Chlamydomonas reinhardtii with a large-subunit V331A mutation==
<StructureSection load='2v63' size='340' side='right'caption='[[2v63]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2v63]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V63 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V63 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2v63]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V63 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><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]] 1.8&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uw9|1uw9]], [[1ir2|1ir2]], [[1uzd|1uzd]], [[1uzh|1uzh]], [[1gk8|1gk8]], [[2v67|2v67]], [[2v68|2v68]], [[2v69|2v69]], [[2v6a|2v6a]]</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=2v63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v63 OCA], [https://pdbe.org/2v63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v63 RCSB], [https://www.ebi.ac.uk/pdbsum/2v63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v63 ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </span></td></tr>
</table>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v63 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v63 RCSB], [http://www.ebi.ac.uk/pdbsum/2v63 PDBsum]</span></td></tr>
== Function ==
<table>
[https://www.uniprot.org/uniprot/RBS1_CHLRE RBS1_CHLRE] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v6/2v63_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v6/2v63_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata 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=2v63 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2v63" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[RuBisCO|RuBisCO]]
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Chlamydomonas reinhardtii]]
[[Category: Chlamydomonas reinhardtii]]
[[Category: Ribulose-bisphosphate carboxylase]]
[[Category: Large Structures]]
[[Category: Andersson, I.]]
[[Category: Andersson I]]
[[Category: Karkehabadi, S.]]
[[Category: Karkehabadi S]]
[[Category: Satagopan, S.]]
[[Category: Satagopagan S]]
[[Category: Spreitzer, R J.]]
[[Category: Spreitzer RJ]]
[[Category: Taylor, T C.]]
[[Category: Taylor TC]]
[[Category: Calvin cycle]]
[[Category: Carbon dioxide fixation]]
[[Category: Chloroplast]]
[[Category: Co2/o2 specificity]]
[[Category: Hydroxylation]]
[[Category: Large subunit loop 6 mutation]]
[[Category: Lyase]]
[[Category: Magnesium]]
[[Category: Metal-binding]]
[[Category: Methylation]]
[[Category: Monooxygenase]]
[[Category: Oxidoreductase]]
[[Category: Photorespiration]]
[[Category: Photosynthesis]]
[[Category: Rubisco]]
[[Category: Transit peptide]]

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