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| | <SX load='5nv3' size='340' side='right' viewer='molstar' caption='[[5nv3]], [[Resolution|resolution]] 3.39Å' scene=''> | | <SX load='5nv3' size='340' side='right' viewer='molstar' caption='[[5nv3]], [[Resolution|resolution]] 3.39Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nv3]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NV3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NV3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nv3]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NV3 FirstGlance]. <br> |
| - | </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=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">Electron Microscopy, [[Resolution|Resolution]] 3.39Å</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cbbL, cbbL1, rbcL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907]), cbbS, rbcS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907])</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=5nv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nv3 OCA], [https://pdbe.org/5nv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nv3 RCSB], [https://www.ebi.ac.uk/pdbsum/5nv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nv3 ProSAT]</span></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'>[http://proteopedia.org/fgij/fg.htm?mol=5nv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nv3 OCA], [http://pdbe.org/5nv3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nv3 RCSB], [http://www.ebi.ac.uk/pdbsum/5nv3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nv3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RBL1_RHOSH RBL1_RHOSH]] 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. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]<ref>PMID:9882445</ref> [[http://www.uniprot.org/uniprot/RBS1_RHOSH RBS1_RHOSH]] 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. Both reactions occur simultaneously and in competition at the same active site.<ref>PMID:9882445</ref> | + | [https://www.uniprot.org/uniprot/RBL1_CERSP RBL1_CERSP] 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. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]<ref>PMID:9882445</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Rhodococcus capsulatus molisch 1907]] | + | [[Category: Cereibacter sphaeroides]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ribulose-bisphosphate carboxylase]]
| + | [[Category: Bracher A]] |
| - | [[Category: Bracher, A]] | + | [[Category: Ciniawsky S]] |
| - | [[Category: Ciniawsky, S]] | + | [[Category: Hartl FU]] |
| - | [[Category: Hartl, F U]] | + | [[Category: Hayer-Hartl M]] |
| - | [[Category: Hayer-Hartl, M]] | + | [[Category: Milicic G]] |
| - | [[Category: Milicic, G]] | + | [[Category: Wendler P]] |
| - | [[Category: Wendler, P]] | + | |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
RBL1_CERSP 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. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338][1]
Publication Abstract from PubMed
How AAA+ chaperones conformationally remodel specific target proteins in an ATP-dependent manner is not well understood. Here, we investigated the mechanism of the AAA+ protein Rubisco activase (Rca) in metabolic repair of the photosynthetic enzyme Rubisco, a complex of eight large (RbcL) and eight small (RbcS) subunits containing eight catalytic sites. Rubisco is prone to inhibition by tight-binding sugar phosphates, whose removal is catalyzed by Rca. We engineered a stable Rca hexamer ring and analyzed its functional interaction with Rubisco. Hydrogen/deuterium exchange and chemical crosslinking showed that Rca structurally destabilizes elements of the Rubisco active site with remarkable selectivity. Cryo-electron microscopy revealed that Rca docks onto Rubisco over one active site at a time, positioning the C-terminal strand of RbcL, which stabilizes the catalytic center, for access to the Rca hexamer pore. The pulling force of Rca is fine-tuned to avoid global destabilization and allow for precise enzyme repair.
Mechanism of Enzyme Repair by the AAA+ Chaperone Rubisco Activase.,Bhat JY, Milicic G, Thieulin-Pardo G, Bracher A, Maxwell A, Ciniawsky S, Mueller-Cajar O, Engen JR, Hartl FU, Wendler P, Hayer-Hartl M Mol Cell. 2017 Jul 20. pii: S1097-2765(17)30498-7. doi:, 10.1016/j.molcel.2017.07.004. PMID:28803776[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Horken KM, Tabita FR. Closely related form I ribulose bisphosphate carboxylase/oxygenase molecules that possess different CO2/O2 substrate specificities. Arch Biochem Biophys. 1999 Jan 15;361(2):183-94. PMID:9882445 doi:http://dx.doi.org/S0003-9861(98)90979-1
- ↑ Bhat JY, Milicic G, Thieulin-Pardo G, Bracher A, Maxwell A, Ciniawsky S, Mueller-Cajar O, Engen JR, Hartl FU, Wendler P, Hayer-Hartl M. Mechanism of Enzyme Repair by the AAA+ Chaperone Rubisco Activase. Mol Cell. 2017 Jul 20. pii: S1097-2765(17)30498-7. doi:, 10.1016/j.molcel.2017.07.004. PMID:28803776 doi:http://dx.doi.org/10.1016/j.molcel.2017.07.004
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