5lb9
From Proteopedia
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==Structure of the T175V Etr1p mutant in the monoclinic form P21== | ==Structure of the T175V Etr1p mutant in the monoclinic form P21== | ||
| - | <StructureSection load='5lb9' size='340' side='right' caption='[[5lb9]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='5lb9' size='340' side='right'caption='[[5lb9]], [[Resolution|resolution]] 2.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5lb9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LB9 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5lb9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LB9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5lb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lb9 OCA], [https://pdbe.org/5lb9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lb9 RCSB], [https://www.ebi.ac.uk/pdbsum/5lb9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lb9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ETR1_CANTR ETR1_CANTR] Required for respiration and the maintenance of the mitochondrial compartment. May have a role in the mitochondrial synthesis of fatty acids.<ref>PMID:11509667</ref> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Enzymes are highly specific biocatalysts, yet they can promote unwanted side reactions. Here we investigated the factors that direct catalysis in the enoyl-thioester reductase Etr1p. We show that a single conserved threonine is essential to suppress the formation of a side product that would otherwise act as a high-affinity inhibitor of the enzyme. Substitution of this threonine with isosteric valine increases side-product formation by more than six orders of magnitude, while decreasing turnover frequency by only one order of magnitude. Our results show that the promotion of wanted reactions and the suppression of unwanted side reactions operate independently at the active site of Etr1p, and that the active suppression of side reactions is highly conserved in the family of medium-chain dehydrogenases/reductases (MDRs). Our discovery emphasizes the fact that the active destabilization of competing transition states is an important factor during catalysis that has implications for the understanding and the de novo design of enzymes. | ||
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| + | A conserved threonine prevents self-intoxication of enoyl-thioester reductases.,Rosenthal RG, Vogeli B, Wagner T, Shima S, Erb TJ Nat Chem Biol. 2017 May 15. doi: 10.1038/nchembio.2375. PMID:28504678<ref>PMID:28504678</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5lb9" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Candida tropicalis]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Erb TJ]] |
| - | [[Category: | + | [[Category: Rosenthal RG]] |
| - | [[Category: | + | [[Category: Shima S]] |
| - | [[Category: | + | [[Category: Voegeli B]] |
| - | [[Category: | + | [[Category: Wagner T]] |
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Current revision
Structure of the T175V Etr1p mutant in the monoclinic form P21
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