4was

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==STRUCTURE OF THE ETR1P/NADP/CROTONYL-COA COMPLEX==
==STRUCTURE OF THE ETR1P/NADP/CROTONYL-COA COMPLEX==
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<StructureSection load='4was' size='340' side='right' caption='[[4was]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='4was' size='340' side='right'caption='[[4was]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4was]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WAS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4was]] is a 3 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=4WAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WAS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COO:CROTONYL+COENZYME+A'>COO</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4w99|4w99]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COO:CROTONYL+COENZYME+A'>COO</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4was FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4was OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4was RCSB], [http://www.ebi.ac.uk/pdbsum/4was PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4was FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4was OCA], [https://pdbe.org/4was PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4was RCSB], [https://www.ebi.ac.uk/pdbsum/4was PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4was ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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An improved understanding of enzymes' catalytic proficiency and stereoselectivity would further enable applications in chemistry, biocatalysis and industrial biotechnology. We use a chemical probe to dissect individual catalytic steps of enoyl-thioester reductases (Etrs), validating an active site tyrosine as the cryptic proton donor and explaining how it had eluded definitive identification. This information enabled the rational redesign of Etr, yielding mutants that create products with inverted stereochemistry at wild type-like turnover frequency.
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The use of ene adducts to study and engineer enoyl-thioester reductases.,Rosenthal RG, Vogeli B, Quade N, Capitani G, Kiefer P, Vorholt JA, Ebert MO, Erb TJ Nat Chem Biol. 2015 Apr 13. doi: 10.1038/nchembio.1794. PMID:25867044<ref>PMID:25867044</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4was" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Capitani, G]]
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[[Category: Candida tropicalis]]
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[[Category: Erb, T J]]
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[[Category: Large Structures]]
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[[Category: Quade, N]]
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[[Category: Capitani G]]
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[[Category: Rosenthal, R]]
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[[Category: Erb TJ]]
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[[Category: Voegeli, B]]
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[[Category: Quade N]]
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[[Category: Mitochondrial fatty acid synthesis]]
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[[Category: Rosenthal R]]
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[[Category: Oxidoreductase]]
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[[Category: Voegeli B]]

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STRUCTURE OF THE ETR1P/NADP/CROTONYL-COA COMPLEX

PDB ID 4was

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