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| | <StructureSection load='6kkm' size='340' side='right'caption='[[6kkm]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='6kkm' size='340' side='right'caption='[[6kkm]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6kkm]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KKM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KKM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6kkm]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KKM FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">all5250 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=103690 Anabaena 7120]), cbbL, rbc, rbcA, rbcL, alr1524 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=103690 Anabaena 7120])</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]] 3Å</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=6kkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kkm OCA], [https://pdbe.org/6kkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kkm RCSB], [https://www.ebi.ac.uk/pdbsum/6kkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kkm ProSAT]</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=6kkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kkm OCA], [http://pdbe.org/6kkm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kkm RCSB], [http://www.ebi.ac.uk/pdbsum/6kkm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kkm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RBL_NOSS1 RBL_NOSS1]] 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/RAF1_NOSS1 RAF1_NOSS1] A major RuBisCO chaperone. Acts after GroEL-GroES chaperonin to fold and/or assemble the large subunit of RuBisCO (ccbL, rbcL). Cooperates with RbcX in RbcL folding, plays the major role in assembly of dimers into RbcL(8)-Raf1(8) intermediate complexes. RbcS replaces Raf1, leading to holoenzyme formation.[HAMAP-Rule:MF_00856]<ref>PMID:32451445</ref> In vitro acts as an antagonist to CcmM35, suggesting it might regulate RuBisCO condensation and decondensation.<ref>PMID:32451445</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6kkm" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6kkm" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[RuBisCO 3D structures|RuBisCO 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anabaena 7120]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ribulose-bisphosphate carboxylase]] | + | [[Category: Nostoc sp. PCC 7120 = FACHB-418]] |
| - | [[Category: Chen, Y]] | + | [[Category: Chen Y]] |
| - | [[Category: Jiang, Y L]] | + | [[Category: Jiang YL]] |
| - | [[Category: Kong, W W]] | + | [[Category: Kong WW]] |
| - | [[Category: Xia, L Y]] | + | [[Category: Xia LY]] |
| - | [[Category: Zhou, C Z]] | + | [[Category: Zhou CZ]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Chaperone-photosynthesis complex]]
| + | |
| - | [[Category: Raf1]]
| + | |
| - | [[Category: Rbcl]]
| + | |
| - | [[Category: Rubisco]]
| + | |
| Structural highlights
Function
RAF1_NOSS1 A major RuBisCO chaperone. Acts after GroEL-GroES chaperonin to fold and/or assemble the large subunit of RuBisCO (ccbL, rbcL). Cooperates with RbcX in RbcL folding, plays the major role in assembly of dimers into RbcL(8)-Raf1(8) intermediate complexes. RbcS replaces Raf1, leading to holoenzyme formation.[HAMAP-Rule:MF_00856][1] In vitro acts as an antagonist to CcmM35, suggesting it might regulate RuBisCO condensation and decondensation.[2]
Publication Abstract from PubMed
The folding and assembly of RuBisCO, the most abundant enzyme in nature, needs a series of chaperones, including the RuBisCO accumulation factor Raf1, which is highly conserved in cyanobacteria and plants. Here, we report the crystal structures of Raf1 from cyanobacteria Anabaena sp. PCC 7120 and its complex with RuBisCO large subunit RbcL. Structural analyses and biochemical assays reveal that each Raf1 dimer captures an RbcL dimer, with the C-terminal tail inserting into the catalytic pocket, and further mediates the assembly of RbcL dimers to form the octameric core of RuBisCO. Furthermore, the cryo-electron microscopy structures of the RbcL-Raf1-RbcS assembly intermediates enable us to see a dynamic assembly process from RbcL8Raf18 to the holoenzyme RbcL8RbcS8. In vitro assays also indicate that Raf1 can attenuate and reverse CcmM-mediated cyanobacterial RuBisCO condensation. Combined with previous findings, we propose a putative model for the assembly of cyanobacterial RuBisCO coordinated by the chaperone Raf1.
Molecular basis for the assembly of RuBisCO assisted by the chaperone Raf1.,Xia LY, Jiang YL, Kong WW, Sun H, Li WF, Chen Y, Zhou CZ Nat Plants. 2020 May 25. pii: 10.1038/s41477-020-0665-8. doi:, 10.1038/s41477-020-0665-8. PMID:32451445[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Xia LY, Jiang YL, Kong WW, Sun H, Li WF, Chen Y, Zhou CZ. Molecular basis for the assembly of RuBisCO assisted by the chaperone Raf1. Nat Plants. 2020 May 25. pii: 10.1038/s41477-020-0665-8. doi:, 10.1038/s41477-020-0665-8. PMID:32451445 doi:http://dx.doi.org/10.1038/s41477-020-0665-8
- ↑ Xia LY, Jiang YL, Kong WW, Sun H, Li WF, Chen Y, Zhou CZ. Molecular basis for the assembly of RuBisCO assisted by the chaperone Raf1. Nat Plants. 2020 May 25. pii: 10.1038/s41477-020-0665-8. doi:, 10.1038/s41477-020-0665-8. PMID:32451445 doi:http://dx.doi.org/10.1038/s41477-020-0665-8
- ↑ Xia LY, Jiang YL, Kong WW, Sun H, Li WF, Chen Y, Zhou CZ. Molecular basis for the assembly of RuBisCO assisted by the chaperone Raf1. Nat Plants. 2020 May 25. pii: 10.1038/s41477-020-0665-8. doi:, 10.1038/s41477-020-0665-8. PMID:32451445 doi:http://dx.doi.org/10.1038/s41477-020-0665-8
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