View source for 6juj


==Crystal structure of Formate dehydrogenase mutant V198I/C256I/P260S/E261P/S381N/S383F from Pseudomonas sp. 101in complex with non-natural cofactor Nicotinamide Cytosine Dinucleotide==
<StructureSection load='6juj' size='340' side='right'caption='[[6juj]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6juj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._101 Pseudomonas sp. 101]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JUJ 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]] 2.183&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A7R:[[(2S,3S,4R,5S)-5-(3-aminocarbonylpyridin-1-ium-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]+[(2S,3S,4R,5S)-5-(4-azanyl-2-oxidanylidene-pyrimidin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+hydrogen+phosphate'>A7R</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6juj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6juj OCA], [https://pdbe.org/6juj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6juj RCSB], [https://www.ebi.ac.uk/pdbsum/6juj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6juj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FDH_PSESR FDH_PSESR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Formate dehydrogenase (FDH) has been widely used for the regeneration of the reduced nicotinamide adenine dinucleotide (NADH). To utilize nicotinamide cytosine dinucleotide (NCD) as a non-natural redox cofactor, it remains challenging as NCDH, the reduced form of NCD, has to be efficiently regenerated. Here we demonstrate successful engineering of FDH for NCDH regeneration. Guided by the structural information of FDH from Pseudomonas sp. 101 (pseFDH) and the NAD-pseFDH complex, semi-rational strategies were applied to design mutant libraries and screen for NCD-linked activity. The most active mutant reached a cofactor preference switch from NAD to NCD by 3700-fold. Homology modeling analysis showed that these mutants had reduced cofactor binding pockets and dedicated hydrophobic interactions for NCD. Efficient regeneration of NCDH was implemented by powering an NCD-dependent D-lactate dehydrogenase for stoichiometric and stereospecific reduction of pyruvate to D-lactate at the expense of formate.

Structure-Guided Design of Formate Dehydrogenase for Regeneration of a Non-Natural Redox Cofactor.,Guo X, Wang X, Liu Y, Li Q, Wang J, Liu W, Zhao ZK Chemistry. 2020 Dec 15;26(70):16611-16615. doi: 10.1002/chem.202003102. Epub 2020, Nov 16. PMID:32815230<ref>PMID:32815230</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6juj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Formate dehydrogenase 3D structures|Formate dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas sp. 101]]
[[Category: Feng Y]]
[[Category: Guo X]]
[[Category: Xue S]]
[[Category: Zhao Z]]