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==Crystal structures of (S)-carbonyl reductases from Candida parapsilosis in different oligomerization states== | ==Crystal structures of (S)-carbonyl reductases from Candida parapsilosis in different oligomerization states== | ||
<StructureSection load='7dmg' size='340' side='right'caption='[[7dmg]]' scene=''> | <StructureSection load='7dmg' size='340' side='right'caption='[[7dmg]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DMG FirstGlance]. <br> | <table><tr><td colspan='2'>[[7dmg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DMG FirstGlance]. <br> | ||
</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=7dmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dmg OCA], [https://pdbe.org/7dmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dmg RCSB], [https://www.ebi.ac.uk/pdbsum/7dmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dmg ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=7dmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dmg OCA], [https://pdbe.org/7dmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dmg RCSB], [https://www.ebi.ac.uk/pdbsum/7dmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dmg ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The evolutionary benefit accounting for widespread conservation of oligomeric structures in proteins lacking evidence of intersubunit cooperativity remains unclear. Here, crystal and cryo-EM structures, and enzymological data, demonstrate that a conserved tetramer interface maintains the active-site structure in one such class of proteins, the short-chain dehydrogenase/reductase (SDR) superfamily. Phylogenetic comparisons support a significantly longer polypeptide being required to maintain an equivalent active-site structure in the context of a single subunit. Oligomerization therefore enhances evolutionary fitness by reducing the metabolic cost of enzyme biosynthesis. The large surface area of the structure-stabilizing oligomeric interface yields a synergistic gain in fitness by increasing tolerance to activity-enhancing yet destabilizing mutations. We demonstrate that two paralogous SDR superfamily enzymes with different specificities can form mixed heterotetramers that combine their individual enzymological properties. This suggests that oligomerization can also diversify the functions generated by a given metabolic investment, enhancing the fitness advantage provided by this architectural strategy. | |||
Oligomeric interactions maintain active-site structure in a noncooperative enzyme family.,Li Y, Zhang R, Wang C, Forouhar F, Clarke OB, Vorobiev S, Singh S, Montelione GT, Szyperski T, Xu Y, Hunt JF EMBO J. 2022 Jul 8:e108368. doi: 10.15252/embj.2021108368. PMID:35801308<ref>PMID:35801308</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7dmg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Forouhar F]] | [[Category: Forouhar, F]] | ||
[[Category: Hunt | [[Category: Hunt, J F]] | ||
[[Category: Li | [[Category: Li, Y H]] | ||
[[Category: Montelione | [[Category: Montelione, G T]] | ||
[[Category: Szyperski T]] | [[Category: Szyperski, T]] | ||
[[Category: Wang C]] | [[Category: Wang, C]] | ||
[[Category: Xu Y]] | [[Category: Xu, Y]] | ||
[[Category: Zhang | [[Category: Zhang, R Z]] | ||
[[Category: Oxidoreductase]] | |||
[[Category: Rossmann fold]] | |||
[[Category: Tag-free]] | |||
[[Category: Tetramer]] | |||
[[Category: Wild type with nadph]] | |||
Revision as of 21:12, 27 July 2022
Crystal structures of (S)-carbonyl reductases from Candida parapsilosis in different oligomerization statesCrystal structures of (S)-carbonyl reductases from Candida parapsilosis in different oligomerization states
Structural highlights
Publication Abstract from PubMedThe evolutionary benefit accounting for widespread conservation of oligomeric structures in proteins lacking evidence of intersubunit cooperativity remains unclear. Here, crystal and cryo-EM structures, and enzymological data, demonstrate that a conserved tetramer interface maintains the active-site structure in one such class of proteins, the short-chain dehydrogenase/reductase (SDR) superfamily. Phylogenetic comparisons support a significantly longer polypeptide being required to maintain an equivalent active-site structure in the context of a single subunit. Oligomerization therefore enhances evolutionary fitness by reducing the metabolic cost of enzyme biosynthesis. The large surface area of the structure-stabilizing oligomeric interface yields a synergistic gain in fitness by increasing tolerance to activity-enhancing yet destabilizing mutations. We demonstrate that two paralogous SDR superfamily enzymes with different specificities can form mixed heterotetramers that combine their individual enzymological properties. This suggests that oligomerization can also diversify the functions generated by a given metabolic investment, enhancing the fitness advantage provided by this architectural strategy. Oligomeric interactions maintain active-site structure in a noncooperative enzyme family.,Li Y, Zhang R, Wang C, Forouhar F, Clarke OB, Vorobiev S, Singh S, Montelione GT, Szyperski T, Xu Y, Hunt JF EMBO J. 2022 Jul 8:e108368. doi: 10.15252/embj.2021108368. PMID:35801308[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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