7qvi: Difference between revisions

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New page: '''Unreleased structure''' The entry 7qvi is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 7qvi is ON HOLD
==Fiber-forming RubisCO derived from ancestral sequence reconstruction and rational engineering==
<StructureSection load='7qvi' size='340' side='right'caption='[[7qvi]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7qvi]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QVI 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=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=7qvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qvi OCA], [https://pdbe.org/7qvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qvi RCSB], [https://www.ebi.ac.uk/pdbsum/7qvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qvi ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The evolution of ribulose-1,5-bisphosphate carboxylase/oxygenases (Rubiscos) that discriminate strongly between their substrate carbon dioxide and the undesired side substrate dioxygen was an important event for photosynthetic organisms adapting to an oxygenated environment. We use ancestral sequence reconstruction to recapitulate this event. We show that Rubisco increased its specificity and carboxylation efficiency through the gain of an accessory subunit before atmospheric oxygen was present. Using structural and biochemical approaches, we retrace how this subunit was gained and became essential. Our work illuminates the emergence of an adaptation to rising ambient oxygen levels, provides a template for investigating the function of interactions that have remained elusive because of their essentiality, and sheds light on the determinants of specificity in Rubisco.


Authors:  
Evolution of increased complexity and specificity at the dawn of form I Rubiscos.,Schulz L, Guo Z, Zarzycki J, Steinchen W, Schuller JM, Heimerl T, Prinz S, Mueller-Cajar O, Erb TJ, Hochberg GKA Science. 2022 Oct 14;378(6616):155-160. doi: 10.1126/science.abq1416. Epub 2022, Oct 13. PMID:36227987<ref>PMID:36227987</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 7qvi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Erb TJ]]
[[Category: Hochberg GKA]]
[[Category: Prinz S]]
[[Category: Schuller JM]]
[[Category: Schulz L]]
[[Category: Zarzycki J]]

Latest revision as of 09:25, 26 October 2022

Fiber-forming RubisCO derived from ancestral sequence reconstruction and rational engineeringFiber-forming RubisCO derived from ancestral sequence reconstruction and rational engineering

Structural highlights

7qvi is a 16 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

The evolution of ribulose-1,5-bisphosphate carboxylase/oxygenases (Rubiscos) that discriminate strongly between their substrate carbon dioxide and the undesired side substrate dioxygen was an important event for photosynthetic organisms adapting to an oxygenated environment. We use ancestral sequence reconstruction to recapitulate this event. We show that Rubisco increased its specificity and carboxylation efficiency through the gain of an accessory subunit before atmospheric oxygen was present. Using structural and biochemical approaches, we retrace how this subunit was gained and became essential. Our work illuminates the emergence of an adaptation to rising ambient oxygen levels, provides a template for investigating the function of interactions that have remained elusive because of their essentiality, and sheds light on the determinants of specificity in Rubisco.

Evolution of increased complexity and specificity at the dawn of form I Rubiscos.,Schulz L, Guo Z, Zarzycki J, Steinchen W, Schuller JM, Heimerl T, Prinz S, Mueller-Cajar O, Erb TJ, Hochberg GKA Science. 2022 Oct 14;378(6616):155-160. doi: 10.1126/science.abq1416. Epub 2022, Oct 13. PMID:36227987[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Schulz L, Guo Z, Zarzycki J, Steinchen W, Schuller JM, Heimerl T, Prinz S, Mueller-Cajar O, Erb TJ, Hochberg GKA. Evolution of increased complexity and specificity at the dawn of form I Rubiscos. Science. 2022 Oct 14;378(6616):155-160. doi: 10.1126/science.abq1416. Epub 2022, Oct 13. PMID:36227987 doi:http://dx.doi.org/10.1126/science.abq1416

7qvi, resolution 3.00Å

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OCA