View source for 5cpn


==Crystal structure of XenA from Pseudomonas putida in complex with an NADH mimic (mAc)==
<StructureSection load='5cpn' size='340' side='right'caption='[[5cpn]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cpn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CPN 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=531:1-[(3S)-1-BENZYLPIPERIDIN-3-YL]ETHANONE'>531</scene>, <scene name='pdbligand=FNR:1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL'>FNR</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=5cpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cpn OCA], [https://pdbe.org/5cpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cpn RCSB], [https://www.ebi.ac.uk/pdbsum/5cpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cpn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9R9V9_PSEPU Q9R9V9_PSEPU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The search for affordable, green biocatalytic processes is a challenge for chemicals manufacture. Redox biotransformations are potentially attractive, but they rely on unstable and expensive nicotinamide coenzymes that have prevented their widespread exploitation. Stoichiometric use of natural coenzymes is not viable economically, and the instability of these molecules hinders catalytic processes that employ coenzyme recycling. Here, we investigate the efficiency of man-made synthetic biomimetics of the natural coenzymes NAD(P)H in redox biocatalysis. Extensive studies with a range of oxidoreductases belonging to the "ene" reductase family show that these biomimetics are excellent analogues of the natural coenzymes, revealed also in crystal structures of the ene reductase XenA with selected biomimetics. In selected cases, these biomimetics outperform the natural coenzymes. "Better-than-Nature" biomimetics should find widespread application in fine and specialty chemicals production by harnessing the power of high stereo-, regio-, and chemoselective redox biocatalysts and enabling reactions under mild conditions at low cost.

Better than Nature: Nicotinamide Biomimetics That Outperform Natural Coenzymes.,Knaus T, Paul CE, Levy CW, de Vries S, Mutti FG, Hollmann F, Scrutton NS J Am Chem Soc. 2016 Jan 13. PMID:26727612<ref>PMID:26727612</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5cpn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Hollmann F]]
[[Category: Knaus T]]
[[Category: Levy CW]]
[[Category: Mutti FG]]
[[Category: Paul CE]]
[[Category: Scrutton NS]]