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[[Image:1aa1.png|left|200px]]


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==ACTIVATED SPINACH RUBISCO IN COMPLEX WITH THE PRODUCT 3-PHOSPHOGLYCERATE==
The line below this paragraph, containing "STRUCTURE_1aa1", creates the "Structure Box" on the page.
<StructureSection load='1aa1' size='340' side='right'caption='[[1aa1]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1aa1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AA1 FirstGlance]. <br>
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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]] 2.2&#8491;</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=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_1aa1|  PDB=1aa1  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aa1 OCA], [https://pdbe.org/1aa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aa1 RCSB], [https://www.ebi.ac.uk/pdbsum/1aa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aa1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RBL_SPIOL RBL_SPIOL] 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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]
== 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/aa/1aa1_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=1aa1 ConSurf].
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== Publication Abstract from PubMed ==
The crystal structure of an activated complex of ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach and its product 3-phosphoglycerate has been determined to 2.2 A resolution. The structure is of the open form with the active site accessible to the solvent as observed in the structures of the activated ligand-free enzyme and the complex of the activated enzyme with the substrate ribulose-1,5-bisphosphate. Two molecules of 3-phosphoglycerate are bound per active site. The phosphates of both molecules bind approximately at the same position as the phosphates of ribulose-1,5-bisphosphate or the six-carbon intermediate analogue 2-carboxyarabinitol-1,5-bisphosphate, but one product molecule is swung out from the active site with its carboxylate group pointing toward solution. The present structure points to direct participation of the active site side chain of lysine 175 in later stages of catalysis. This possibility is discussed in the light of mutagenesis studies.


===ACTIVATED SPINACH RUBISCO IN COMPLEX WITH THE PRODUCT 3-PHOSPHOGLYCERATE===
Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase.,Taylor TC, Andersson I Biochemistry. 1997 Apr 1;36(13):4041-6. PMID:9092835<ref>PMID:9092835</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1aa1" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_9092835}}, adds the Publication Abstract to the page
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 9092835 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_9092835}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1AA1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AA1 OCA].
 
==Reference==
Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase., Taylor TC, Andersson I, Biochemistry. 1997 Apr 1;36(13):4041-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9092835 9092835]
[[Category: Protein complex]]
[[Category: Ribulose-bisphosphate carboxylase]]
[[Category: Spinacia oleracea]]
[[Category: Spinacia oleracea]]
[[Category: Andersson, I.]]
[[Category: Andersson I]]
[[Category: Taylor, T C.]]
[[Category: Taylor TC]]
[[Category: Oxidoreductase]]
 
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