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| | <StructureSection load='4hhh' size='340' side='right'caption='[[4hhh]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='4hhh' size='340' side='right'caption='[[4hhh]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hhh]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HHH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HHH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hhh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HHH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RUB:RIBULOSE-1,5-DIPHOSPHATE'>RUB</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]] 2.2Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RUB:RIBULOSE-1,5-DIPHOSPHATE'>RUB</scene></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=4hhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hhh OCA], [http://pdbe.org/4hhh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hhh RCSB], [http://www.ebi.ac.uk/pdbsum/4hhh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hhh ProSAT]</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=4hhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hhh OCA], [https://pdbe.org/4hhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hhh RCSB], [https://www.ebi.ac.uk/pdbsum/4hhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hhh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RBL_PEA RBL_PEA]] 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] | + | [https://www.uniprot.org/uniprot/RBL_PEA RBL_PEA] 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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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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: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Pisum sativum]] | | [[Category: Pisum sativum]] |
| - | [[Category: Ribulose-bisphosphate carboxylase]]
| + | [[Category: Didychuk AL]] |
| - | [[Category: Didychuk, A L]] | + | [[Category: Loewen MC]] |
| - | [[Category: Loewen, M C]] | + | [[Category: Loewen PC]] |
| - | [[Category: Loewen, P C]] | + | [[Category: Switala J]] |
| - | [[Category: Switala, J]] | + | |
| - | [[Category: 5-bisphosphate]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Ribulose-1]]
| + | |
| - | [[Category: Rubisco]]
| + | |
| Structural highlights
Function
RBL_PEA 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]
Publication Abstract from PubMed
The first structure of a ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from a pulse crop is reported. Rubisco was purified from Pisum sativum (garden pea) and diffraction-quality crystals were obtained by hanging-drop vapour diffusion in the presence of the substrate ribulose 1,5-bisphosphate. X-ray diffraction data were recorded to 2.20 A resolution from a single crystal at the Canadian Light Source. The overall quaternary structure of non-activated P. sativum Rubisco highlights the conservation of the form I Rubisco hexadecameric complex. The electron density places the substrate in the active site at the interface of the large-subunit dimers. Lys201 in the active site is not carbamylated as expected for this non-activated structure. Some heterogeneity in the small-subunit sequence is noted, as well as possible variations in the conformation and contacts of ribulose 1,5-bisphosphate in the large-subunit active sites. Overall, the active-site conformation most closely correlates with the `closed' conformation observed in other substrate/inhibitor-bound Rubisco structures.
Structure of Pisum sativum Rubisco with bound ribulose 1,5-bisphosphate.,Loewen PC, Didychuk AL, Switala J, Perez-Luque R, Fita I, Loewen MC Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jan 1;69(Pt 1):10-4. doi: , 10.1107/S1744309112047549. Epub 2012 Dec 25. PMID:23295478[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Loewen PC, Didychuk AL, Switala J, Perez-Luque R, Fita I, Loewen MC. Structure of Pisum sativum Rubisco with bound ribulose 1,5-bisphosphate. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jan 1;69(Pt 1):10-4. doi: , 10.1107/S1744309112047549. Epub 2012 Dec 25. PMID:23295478 doi:http://dx.doi.org/10.1107/S1744309112047549
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