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| | <StructureSection load='1iwa' size='340' side='right'caption='[[1iwa]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='1iwa' size='340' side='right'caption='[[1iwa]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1iwa]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Galdieria_partita Galdieria partita]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IWA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1iwa]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Galdieria_partita Galdieria partita]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IWA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bwv|1bwv]], [[1ej7|1ej7]], [[1ir1|1ir1]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><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>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwa OCA], [https://pdbe.org/1iwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iwa RCSB], [https://www.ebi.ac.uk/pdbsum/1iwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iwa ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwa OCA], [http://pdbe.org/1iwa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iwa RCSB], [http://www.ebi.ac.uk/pdbsum/1iwa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iwa ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/O98949_9RHOD O98949_9RHOD]] 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 (By similarity).[HAMAP-Rule:MF_01338] | + | [https://www.uniprot.org/uniprot/O98949_9RHOD O98949_9RHOD] 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 (By similarity).[HAMAP-Rule:MF_01338] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[RuBisCO|RuBisCO]] | + | *[[RuBisCO 3D structures|RuBisCO 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Galdieria partita]] | | [[Category: Galdieria partita]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ribulose-bisphosphate carboxylase]]
| + | [[Category: Inoue T]] |
| - | [[Category: Inoue, T]] | + | [[Category: Kai Y]] |
| - | [[Category: Kai, Y]] | + | [[Category: Matsumura H]] |
| - | [[Category: Matsumura, H]] | + | [[Category: Mizohata E]] |
| - | [[Category: Mizohata, E]] | + | [[Category: Okano Y]] |
| - | [[Category: Okano, Y]] | + | [[Category: Sugawara H]] |
| - | [[Category: Sugawara, H]] | + | [[Category: Xie Y]] |
| - | [[Category: Xie, Y]] | + | [[Category: Yokota A]] |
| - | [[Category: Yokota, A]] | + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Photosynthesis]]
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| - | [[Category: Rubisco]]
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| Structural highlights
Function
O98949_9RHOD 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 (By similarity).[HAMAP-Rule:MF_01338]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the reactions of carboxylation and oxygenation of ribulose-1,5-bisphosphate. These reactions require that the active site should be closed by a flexible loop (loop 6) of the large subunit. Rubisco from a red alga, Galdieria partita, has the highest specificity for carboxylation reaction among the Rubiscos hitherto reported. The crystal structure of unactivated Galdieria Rubisco has been determined at 2.6 A resolution. The electron density map reveals that a sulfate binds only to the P1 anion-binding site of the active site and the loop 6 is closed. Galdieria Rubisco has a unique hydrogen bond between the main chain oxygen of Val332 on the loop 6 and the epsilon-amino group of Gln386 of the same large subunit. This interaction is likely to be crucial to understanding for stabilizing the loop 6 in the closed state and to making a higher affinity for anionic ligands.
X-ray structure of Galdieria Rubisco complexed with one sulfate ion per active site.,Okano Y, Mizohata E, Xie Y, Matsumura H, Sugawara H, Inoue T, Yokota A, Kai Y FEBS Lett. 2002 Sep 11;527(1-3):33-6. PMID:12220629[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Okano Y, Mizohata E, Xie Y, Matsumura H, Sugawara H, Inoue T, Yokota A, Kai Y. X-ray structure of Galdieria Rubisco complexed with one sulfate ion per active site. FEBS Lett. 2002 Sep 11;527(1-3):33-6. PMID:12220629
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