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1rbl

From Proteopedia

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[[Image:1rbl.gif|left|200px]]<br />
 
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<applet load="1rbl" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rbl, resolution 2.2&Aring;" />
 
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'''STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301'''<br />
 
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==Overview==
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==STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301==
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The structure of an activated quaternary complex of ribulose, 1,5-bisphosphate carboxylase/oxygenase (rubisco) from Synechococcus, PCC6301 has been solved by molecular replacement. The protein crystallizes, in an orthorhombic P2(1)2(1)2(1) unit cell with a complete L(8)S(8), complex consisting of 4608 residues (37 680 non-hydrogen atoms) in the, asymmetric unit. Data were collected both on film and image plate using, synchrotron radiation; there were 218 276 unique reflections in the final, 2.2 A data set. The eightfold non-crystallographic symmetry could be used, both to improve map quality and to reduce the computing requirements of, refinement. The coordinates were refined using strict non-crystallographic, symmetry constraints. The stereochemistry of the final model is good, and, the model has an R value of 20.0% for the reflections between 7 and 2.2 A.
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<StructureSection load='1rbl' size='340' side='right'caption='[[1rbl]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rbl]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_6301 Synechococcus elongatus PCC 6301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RBL 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=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <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=1rbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rbl OCA], [https://pdbe.org/1rbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rbl RCSB], [https://www.ebi.ac.uk/pdbsum/1rbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rbl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RBL_SYNP6 RBL_SYNP6] 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/rb/1rbl_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=1rbl 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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1RBL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.] with MG, CAP 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] Structure known Active Site: 1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RBL 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 determination and refinement of ribulose 1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301., Newman J, Branden CI, Jones TA, Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):548-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299492 15299492]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Synechococcus elongatus PCC 6301]]
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[[Category: Ribulose-bisphosphate carboxylase]]
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[[Category: Branden C-I]]
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[[Category: Synechococcus sp.]]
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[[Category: Gutteridge S]]
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[[Category: Branden, C.I.]]
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[[Category: Jones TA]]
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[[Category: Gutteridge, S.]]
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[[Category: Newman J]]
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[[Category: Jones, T.A.]]
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[[Category: Newman, J.]]
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[[Category: CAP]]
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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 Mon Nov 5 12:31:47 2007''
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Current revision

STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301

PDB ID 1rbl

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