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8u66
From Proteopedia
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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=8u66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8u66 OCA], [https://pdbe.org/8u66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8u66 RCSB], [https://www.ebi.ac.uk/pdbsum/8u66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8u66 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=8u66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8u66 OCA], [https://pdbe.org/8u66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8u66 RCSB], [https://www.ebi.ac.uk/pdbsum/8u66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8u66 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0AAJ6N6K7_9FIRM A0AAJ6N6K7_9FIRM] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The enzyme rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) catalyzes the majority of biological carbon fixation on Earth. Although the vast majority of rubiscos across the tree of life assemble as homo-oligomers, the globally predominant form I enzyme-found in plants, algae, and cyanobacteria-forms a unique hetero-oligomeric complex. The recent discovery of a homo-oligomeric sister group to form I rubisco (named form I') has filled a key gap in our understanding of the enigmatic origins of the form I clade. However, to elucidate the series of molecular events leading to the evolution of form I rubisco, we must examine more distantly related sibling clades to contextualize the molecular features distinguishing form I and form I' rubiscos. Here, we present a comparative structural study retracing the evolutionary history of rubisco that reveals a complex structural trajectory leading to the ultimate hetero-oligomerization of the form I clade. We structurally characterize the oligomeric states of deep-branching form Ialpha and I'' rubiscos recently discovered from metagenomes, which represent key evolutionary intermediates preceding the form I clade. We further solve the structure of form I'' rubisco, revealing the molecular determinants that likely primed the enzyme core for the transition from a homo-oligomer to a hetero-oligomer. Our findings yield new insight into the evolutionary trajectory underpinning the adoption and entrenchment of the prevalent assembly of form I rubisco, providing additional context when viewing the enzyme family through the broader lens of protein evolution. | ||
| + | |||
| + | Deep-branching evolutionary intermediates reveal structural origins of form I rubisco.,Liu AK, Kaeser B, Chen L, West-Roberts J, Taylor-Kearney LJ, Lavy A, Gunzing D, Li WJ, Hammel M, Nogales E, Banfield JF, Shih PM Curr Biol. 2023 Dec 18;33(24):5316-5325.e3. doi: 10.1016/j.cub.2023.10.053. Epub , 2023 Nov 17. PMID:37979578<ref>PMID:37979578</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8u66" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Firmicutes Rubisco
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