View source for 6qkg


==2-Naphthoyl-CoA Reductase(NCR)==
<StructureSection load='6qkg' size='340' side='right'caption='[[6qkg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qkg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacterium_enrichment_culture_clone_N47 Bacterium enrichment culture clone N47]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QKG 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=6qkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qkg OCA], [https://pdbe.org/6qkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qkg RCSB], [https://www.ebi.ac.uk/pdbsum/6qkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qkg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E1YD54_9BACT E1YD54_9BACT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hydride transfers play a crucial role in a multitude of biological redox reactions and are mediated by flavin, deazaflavin or nicotinamide adenine dinucleotide cofactors at standard redox potentials ranging from 0 to -340 mV. 2-Naphthoyl-CoA reductase, a key enzyme of oxygen-independent bacterial naphthalene degradation, uses a low-potential one-electron donor for the two-electron dearomatization of its substrate below the redox limit of known biological hydride transfer processes at E degrees ' = -493 mV. Here we demonstrate by X-ray structural analyses, QM/MM computational studies, and multiple spectroscopy/activity based titrations that highly cooperative electron transfer (n = 3) from a low-potential one-electron (FAD) to a two-electron (FMN) transferring flavin cofactor is the key to overcome the resonance stabilized aromatic system by hydride transfer in a highly hydrophobic pocket. The results evidence how the protein environment inversely functionalizes two flavins to switch from low-potential one-electron to hydride transfer at the thermodynamic limit of flavin redox chemistry.

Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors.,Willistein M, Bechtel DF, Muller CS, Demmer U, Heimann L, Kayastha K, Schunemann V, Pierik AJ, Ullmann GM, Ermler U, Boll M Nat Commun. 2019 May 6;10(1):2074. doi: 10.1038/s41467-019-10078-3. PMID:31061390<ref>PMID:31061390</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qkg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacterium enrichment culture clone N47]]
[[Category: Large Structures]]
[[Category: Ermler U]]
[[Category: Kayastha K]]