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1aus

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(New page: 200px<br /><applet load="1aus" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aus, resolution 2.2&Aring;" /> '''ACTIVATED UNLIGANDED ...)
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[[Image:1aus.gif|left|200px]]<br /><applet load="1aus" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1aus, resolution 2.2&Aring;" />
 
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'''ACTIVATED UNLIGANDED SPINACH RUBISCO'''<br />
 
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==Overview==
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==ACTIVATED UNLIGANDED SPINACH RUBISCO==
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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.
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<StructureSection load='1aus' size='340' side='right'caption='[[1aus]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1aus]] 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=1AUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AUS 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=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aus OCA], [https://pdbe.org/1aus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aus RCSB], [https://www.ebi.ac.uk/pdbsum/1aus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aus ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/1aus_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1aus ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1AUS 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 FMT 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AUS OCA].
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*[[RuBisCO 3D structures|RuBisCO 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Ribulose-bisphosphate carboxylase]]
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[[Category: Spinacia oleracea]]
[[Category: Spinacia oleracea]]
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[[Category: Andersson, I.]]
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[[Category: Andersson I]]
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[[Category: Taylor, T.C.]]
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[[Category: Taylor TC]]
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[[Category: FMT]]
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[[Category: MG]]
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[[Category: lyase (carbon-carbon)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:08:37 2007''
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Current revision

ACTIVATED UNLIGANDED SPINACH RUBISCO

PDB ID 1aus

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