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| | <StructureSection load='6ura' size='340' side='right'caption='[[6ura]], [[Resolution|resolution]] 2.17Å' scene=''> | | <StructureSection load='6ura' size='340' side='right'caption='[[6ura]], [[Resolution|resolution]] 2.17Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ura]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"candidatus_promineofilum_breve"_mcilroy_et_al._2016 "candidatus promineofilum breve" mcilroy et al. 2016]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6URA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6URA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ura]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Promineofilum_breve Candidatus Promineofilum breve]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6URA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6URA FirstGlance]. <br> |
| - | </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=MG:MAGNESIUM+ION'>MG</scene></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]] 2.17Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cbbL, CFX0092_B0544 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1806508 "Candidatus Promineofilum breve" McIlroy et al. 2016])</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=6ura FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ura OCA], [https://pdbe.org/6ura PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ura RCSB], [https://www.ebi.ac.uk/pdbsum/6ura PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ura ProSAT]</span></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'>[http://proteopedia.org/fgij/fg.htm?mol=6ura FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ura OCA], [http://pdbe.org/6ura PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ura RCSB], [http://www.ebi.ac.uk/pdbsum/6ura PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ura ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A160T9D2_9CHLR A0A160T9D2_9CHLR] |
| | <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 6ura" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6ura" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[RuBisCO 3D structures|RuBisCO 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Candidatus promineofilum breve mcilroy et al. 2016]] | + | [[Category: Candidatus Promineofilum breve]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ribulose-bisphosphate carboxylase]]
| + | [[Category: Adams PD]] |
| - | [[Category: Adams, P D]] | + | [[Category: Banda DM]] |
| - | [[Category: Banda, D M]] | + | [[Category: Liu AK]] |
| - | [[Category: Liu, A K]] | + | [[Category: Pereira JH]] |
| - | [[Category: Pereira, J H]] | + | [[Category: Shih PM]] |
| - | [[Category: Shih, P M]] | + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Rubisco carboxylase]]
| + | |
| Structural highlights
Function
A0A160T9D2_9CHLR
Publication Abstract from PubMed
Rubisco sustains the biosphere through the fixation of CO2 into biomass. In plants and cyanobacteria, form I Rubisco is structurally comprised of large and small subunits, whereas all other Rubisco forms lack small subunits. The rise of the form I complex through the innovation of small subunits represents a key, yet poorly understood, transition in Rubisco's evolution. Through metagenomic analyses, we discovered a previously uncharacterized clade sister to form I Rubisco that evolved without small subunits. This clade diverged before the evolution of cyanobacteria and the origin of the small subunit; thus, it provides a unique reference point to advance our understanding of form I Rubisco evolution. Structural and kinetic data presented here reveal how a proto-form I Rubisco assembled and functioned without the structural stability imparted from small subunits. Our findings provide insight into a key evolutionary transition of the most abundant enzyme on Earth and the predominant entry point for nearly all global organic carbon.
Novel bacterial clade reveals origin of form I Rubisco.,Banda DM, Pereira JH, Liu AK, Orr DJ, Hammel M, He C, Parry MAJ, Carmo-Silva E, Adams PD, Banfield JF, Shih PM Nat Plants. 2020 Sep;6(9):1158-1166. doi: 10.1038/s41477-020-00762-4. Epub 2020, Aug 31. PMID:32868887[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Banda DM, Pereira JH, Liu AK, Orr DJ, Hammel M, He C, Parry MAJ, Carmo-Silva E, Adams PD, Banfield JF, Shih PM. Novel bacterial clade reveals origin of form I Rubisco. Nat Plants. 2020 Sep;6(9):1158-1166. doi: 10.1038/s41477-020-00762-4. Epub 2020, Aug 31. PMID:32868887 doi:http://dx.doi.org/10.1038/s41477-020-00762-4
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