View source for 8u66


==Firmicutes Rubisco==
<StructureSection load='8u66' size='340' side='right'caption='[[8u66]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8u66]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Firmicutes Firmicutes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8U66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8U66 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.21&#8491;</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='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>
== 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&reg;/PubMed&reg;, 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__
</StructureSection>
[[Category: Firmicutes]]
[[Category: Large Structures]]
[[Category: Kaeser BP]]
[[Category: Liu AK]]
[[Category: Shih PM]]