View source for 8qzp


==Structure of the non-mitochondrial citrate synthase from Ananas comosus==
<StructureSection load='8qzp' size='340' side='right'caption='[[8qzp]], [[Resolution|resolution]] 4.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8qzp]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Ananas_comosus Ananas comosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QZP 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]] 4.15&#8491;</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=8qzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qzp OCA], [https://pdbe.org/8qzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qzp RCSB], [https://www.ebi.ac.uk/pdbsum/8qzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qzp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A6P5F0R3_ANACO A0A6P5F0R3_ANACO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many enzymes assemble into homomeric protein complexes comprising multiple copies of one protein. Because structural form is usually assumed to follow function in biochemistry, these assemblies are thought to evolve because they provide some functional advantage. In many cases, however, no specific advantage is known and, in some cases, quaternary structure varies among orthologs. This has led to the proposition that self-assembly may instead vary neutrally within protein families. The extent of such variation has been difficult to ascertain because quaternary structure has until recently been difficult to measure on large scales. Here, we employ mass photometry, phylogenetics, and structural biology to interrogate the evolution of homo-oligomeric assembly across the entire phylogeny of prokaryotic citrate synthases - an enzyme with a highly conserved function. We discover a menagerie of different assembly types that come and go over the course of evolution, including cases of parallel evolution and reversions from complex to simple assemblies. Functional experiments in vitro and in vivo indicate that evolutionary transitions between different assemblies do not strongly influence enzyme catalysis. Our work suggests that enzymes can wander relatively freely through a large space of possible assemblies and demonstrates the power of characterizing structure-function relationships across entire phylogenies.

Frequent transitions in self-assembly across the evolution of a central metabolic enzyme.,Sendker FL, Schlotthauer T, Mais CN, Lo YK, Girbig M, Bohn S, Heimerl T, Schindler D, Weinstein A, Metzger BP, Thornton JW, Pillai A, Bange G, Schuller JM, Hochberg GKA bioRxiv [Preprint]. 2024 Jul 7:2024.07.05.602260. doi: 10.1101/2024.07.05.602260. PMID:39005358<ref>PMID:39005358</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8qzp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ananas comosus]]
[[Category: Large Structures]]
[[Category: Bohn S]]
[[Category: Hochberg G]]
[[Category: Lo YK]]
[[Category: Schuller JM]]
[[Category: Sendker FL]]