6jwg

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<StructureSection load='6jwg' size='340' side='right'caption='[[6jwg]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
<StructureSection load='6jwg' size='340' side='right'caption='[[6jwg]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6jwg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Achromobacter_parvulus_t1 Achromobacter parvulus t1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JWG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JWG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6jwg]] 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=6JWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JWG FirstGlance]. <br>
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</td></tr><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=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 2.081&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formate_dehydrogenase Formate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.1.9 1.17.1.9] </span></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6jwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jwg OCA], [http://pdbe.org/6jwg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jwg RCSB], [http://www.ebi.ac.uk/pdbsum/6jwg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jwg ProSAT]</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=6jwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jwg OCA], [https://pdbe.org/6jwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jwg RCSB], [https://www.ebi.ac.uk/pdbsum/6jwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jwg ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FDH_PSESR FDH_PSESR]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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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 6jwg" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Formate dehydrogenase 3D structures|Formate dehydrogenase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Achromobacter parvulus t1]]
 
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[[Category: Formate dehydrogenase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Feng, Y]]
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[[Category: Pseudomonas sp. 101]]
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[[Category: Guo, X]]
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[[Category: Feng Y]]
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[[Category: Xue, S]]
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[[Category: Guo X]]
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[[Category: Zhao, Z]]
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[[Category: Xue S]]
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[[Category: Oxidoreductase]]
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[[Category: Zhao Z]]

Current revision

Crystal structure of Formate dehydrogenase mutant C256I/E261P/S381I from Pseudomonas sp. 101

PDB ID 6jwg

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