8wpz

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Current revision (05:28, 12 June 2024) (edit) (undo)
 
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8wpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wpz OCA], [https://pdbe.org/8wpz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wpz RCSB], [https://www.ebi.ac.uk/pdbsum/8wpz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wpz 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=8wpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wpz OCA], [https://pdbe.org/8wpz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wpz RCSB], [https://www.ebi.ac.uk/pdbsum/8wpz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wpz ProSAT]</span></td></tr>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/RBS_SYNE7 RBS_SYNE7] 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_00859]<ref>PMID:24585024</ref> <ref>PMID:30675061</ref> Beta-carboxysome assembly initiates when soluble RuBisCO aggregates is condensed into a liquid matrix in a pre-carboxysome by the RbcS-like domains of probably both CcmM58 and CcmM35. CcmN interacts with the N-terminus of CcmM58, and then recruits the CcmK2 major shell protein via CcmN's encapsulation peptide. Shell formation requires CcmK proteins and CcmO. CcmL caps the otherwise elongated carboxysome. Once fully encapsulated carboxysomes are formed, they migrate within the cell probably via interactions with the cytoskeleton.<ref>PMID:24267892</ref> <ref>PMID:30675061</ref>
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== Publication Abstract from PubMed ==
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Carboxysomes are large self-assembled microcompartments that serve as the central machinery of a CO(2)-concentrating mechanism (CCM). Biogenesis of carboxysome requires the fine organization of thousands of individual proteins; however, the packaging pattern of internal RuBisCOs remains largely unknown. Here we purified the intact beta-carboxysomes from Synechococcus elongatus PCC 7942 and identified the protein components by mass spectrometry. Cryo-electron tomography combined with subtomogram averaging revealed the general organization pattern of internal RuBisCOs, in which the adjacent RuBisCOs are mainly arranged in three distinct manners: head-to-head, head-to-side, and side-by-side. The RuBisCOs in the outermost layer are regularly aligned along the shell, the majority of which directly interact with the shell. Moreover, statistical analysis enabled us to propose an ideal packaging model of RuBisCOs in the beta-carboxysome. These results provide new insights into the biogenesis of beta-carboxysomes and also advance our understanding of the efficient carbon fixation functionality of carboxysomes.
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Cryo-electron tomography reveals the packaging pattern of RuBisCOs in Synechococcus beta-carboxysome.,Kong WW, Zhu Y, Zhao HR, Du K, Zhou RQ, Li B, Yang F, Hou P, Huang XH, Chen Y, Wang YC, Sun F, Jiang YL, Zhou CZ Structure. 2024 May 27:S0969-2126(24)00184-9. doi: 10.1016/j.str.2024.05.007. PMID:38823379<ref>PMID:38823379</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8wpz" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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Current revision

Cryo-ET structure of RuBisCO at 3.9 angstroms from Synechococcus elongatus PCC 7942

PDB ID 8wpz

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