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| | <StructureSection load='1bwv' size='340' side='right'caption='[[1bwv]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='1bwv' size='340' side='right'caption='[[1bwv]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1bwv]] is a 8 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=1BWV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BWV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bwv]] is a 8 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=1BWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BWV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.4Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | + | <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=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1bwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwv OCA], [https://pdbe.org/1bwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bwv RCSB], [https://www.ebi.ac.uk/pdbsum/1bwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bwv 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=1bwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwv OCA], [http://pdbe.org/1bwv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bwv RCSB], [http://www.ebi.ac.uk/pdbsum/1bwv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bwv 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: Miyake C]] |
| - | [[Category: Miyake, C]] | + | [[Category: Shibata N]] |
| - | [[Category: Shibata, N]] | + | [[Category: Sugawara H]] |
| - | [[Category: Sugawara, H]] | + | [[Category: Yamamoto H]] |
| - | [[Category: Yamamoto, H]] | + | [[Category: Yokota A]] |
| - | [[Category: Yokota, A]] | + | |
| - | [[Category: Carbon dioxide fixation]]
| + | |
| - | [[Category: High specificity factor]]
| + | |
| - | [[Category: Lyase]]
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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, EC 4.1.1. 39) obtained from a thermophilic red alga Galdieria partita has the highest specificity factor of 238 among the Rubiscos hitherto reported. Crystal structure of activated Rubisco from G. partita complexed with the reaction intermediate analogue, 2-carboxyarabinitol 1,5-bisphosphate (2-CABP) has been determined at 2.4-A resolution. Compared with other Rubiscos, different amino residues bring the structural differences in active site, which are marked around the binding sites of P-2 phosphate of 2-CABP. Especially, side chains of His-327 and Arg-295 show the significant differences from those of spinach Rubisco. Moreover, the side chains of Asn-123 and His-294 which are reported to bind the substrate, ribulose 1,5-bisphosphate, form hydrogen bonds characteristic of Galdieria Rubisco. Small subunits of Galdieria Rubisco have more than 30 extra amino acid residues on the C terminus, which make up a hairpin-loop structure to form many interactions with the neighboring small subunits. When the structures of Galdieria and spinach Rubiscos are superimposed, the hairpin region of the neighboring small subunit in Galdieria enzyme and apical portion of insertion residues 52-63 characteristic of small subunits in higher plant enzymes are almost overlapped to each other.
Crystal structure of carboxylase reaction-oriented ribulose 1, 5-bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita.,Sugawara H, Yamamoto H, Shibata N, Inoue T, Okada S, Miyake C, Yokota A, Kai Y J Biol Chem. 1999 May 28;274(22):15655-61. PMID:10336462[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sugawara H, Yamamoto H, Shibata N, Inoue T, Okada S, Miyake C, Yokota A, Kai Y. Crystal structure of carboxylase reaction-oriented ribulose 1, 5-bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita. J Biol Chem. 1999 May 28;274(22):15655-61. PMID:10336462
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