6kkm
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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'> | + | <table><tr><td colspan='2'>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=' | + | </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='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'>[ | + | |
</table> | </table> | ||
- | == 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] | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == 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. | ||
- | + | ==See Also== | |
- | + | *[[RuBisCO 3D structures|RuBisCO 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Anabaena 7120]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | + | [[Category: Chen Y]] | |
- | [[Category: Chen | + | [[Category: Jiang YL]] |
- | [[Category: Jiang | + | [[Category: Kong WW]] |
- | [[Category: Kong | + | [[Category: Xia LY]] |
- | [[Category: Xia | + | [[Category: Zhou CZ]] |
- | [[Category: Zhou | + | |
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Current revision
Crystal structure of RbcL-Raf1 complex from Anabaena sp. PCC 7120
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Categories: Large Structures | Chen Y | Jiang YL | Kong WW | Xia LY | Zhou CZ