View source for 7dlm


==Short chain dehydrogenase (SCR) crystal structure with NADPH==
<StructureSection load='7dlm' size='340' side='right'caption='[[7dlm]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7dlm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_parapsilosis Candida parapsilosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DLM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DLM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.59&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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=7dlm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dlm OCA], [https://pdbe.org/7dlm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dlm RCSB], [https://www.ebi.ac.uk/pdbsum/7dlm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dlm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B2KJ46_CANPA B2KJ46_CANPA] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7dlm" style="background-color:#fffaf0;"></div>

==See Also==
*[[Carbonyl reductase 3D structures|Carbonyl reductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Candida parapsilosis]]
[[Category: Large Structures]]
[[Category: Forouhar F]]
[[Category: Hunt JF]]
[[Category: Li YH]]
[[Category: Montelione GT]]
[[Category: Szyperski T]]
[[Category: Wang C]]
[[Category: Xu Y]]
[[Category: Zhang RZ]]