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==Crystal structure of p-nitrophenol 4-monooxygenase PnpA from Pseudomonas putida DLL-E4==
<StructureSection load='6aio' size='340' side='right'caption='[[6aio]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6aio]] 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=6AIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AIO 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]] 2.04&#8491;</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=6aio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aio OCA], [https://pdbe.org/6aio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6aio RCSB], [https://www.ebi.ac.uk/pdbsum/6aio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6aio ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C6FI48_PSEPU C6FI48_PSEPU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
p-Nitrophenol 4-monooxygenase PnpA, the key enzyme in the hydroquinone pathway of p-nitrophenol (PNP) degradation, catalyzes the monooxygenase reaction of PNP to p-benzoquinone in the presence of FAD and NADH. Here, we determined the first crystal structure of PnpA from Pseudomonas putida DLL-E4 in its apo and FAD-complex forms to a resolution of 2.04A and 2.48A, respectively. The PnpA structure shares a common fold with hydroxybenzoate hydroxylases, despite a low amino sequence identity of 14-18%, confirming it to be a member of the Class A flavoprotein monooxygenases. However, substrate docking studies of PnpA indicated that the residues stabilizing the substrate in an orientation suitable for catalysis are not observed in other homologous hydroxybenzoate hydroxylases, suggesting PnpA employs a unique catalytic mechanism. This work expands our understanding on the reaction mode for this enzyme class.

Crystal structure of p-nitrophenol 4-monooxygenase PnpA from Pseudomonas putida DLL-E4: The key enzyme involved in p-nitrophenol degradation.,Chen Q, Huang Y, Duan Y, Li Z, Cui Z, Liu W Biochem Biophys Res Commun. 2018 Oct 12;504(4):715-720. doi:, 10.1016/j.bbrc.2018.09.040. Epub 2018 Sep 12. PMID:30217456<ref>PMID:30217456</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6aio" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Chen QZ]]
[[Category: Cui ZL]]
[[Category: Duan YJ]]
[[Category: Huang Y]]
[[Category: Li ZK]]
[[Category: Liu WD]]