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[[Image:1aa1.gif|left|200px]]<br />
<applet load="1aa1" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1aa1, resolution 2.2&Aring;" />
'''ACTIVATED SPINACH RUBISCO IN COMPLEX WITH THE PRODUCT 3-PHOSPHOGLYCERATE'''<br />


==Overview==
==ACTIVATED SPINACH RUBISCO IN COMPLEX WITH THE PRODUCT 3-PHOSPHOGLYCERATE==
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.
<StructureSection load='1aa1' size='340' side='right'caption='[[1aa1]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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>
1AA1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea] with MG and 3PG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Structure known Active Sites: ACB, ACE, ACH and ACL. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AA1 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9092835 9092835]
</div>
[[Category: Protein complex]]
<div class="pdbe-citations 1aa1" style="background-color:#fffaf0;"></div>
[[Category: Ribulose-bisphosphate carboxylase]]
 
==See Also==
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Spinacia oleracea]]
[[Category: Spinacia oleracea]]
[[Category: Andersson, I.]]
[[Category: Andersson I]]
[[Category: Taylor, T.C.]]
[[Category: Taylor TC]]
[[Category: 3PG]]
[[Category: MG]]
[[Category: lyase (carbon-carbon)]]
[[Category: oxidoreductase]]
 
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