View source for 5lth


==Crystal structure of the alpha subunit of heme dependent oxidative N-demethylase (HODM) in complex with the dimethylamine substrate==
<StructureSection load='5lth' size='340' side='right'caption='[[5lth]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lth]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_mendocina Pseudomonas mendocina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LTH 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]] 1.76&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMN:DIMETHYLAMINE'>DMN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5lth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lth OCA], [https://pdbe.org/5lth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lth RCSB], [https://www.ebi.ac.uk/pdbsum/5lth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lth ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A4XXY9_PSEMY A4XXY9_PSEMY] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The universal Per-ARNT-Sim (PAS) domain functions as a signal transduction module involved in sensing diverse stimuli such as small molecules, light, redox state and gases. The highly evolvable PAS scaffold can bind a broad range of ligands, including haem, flavins and metal ions. However, although these ligands can support catalytic activity, to our knowledge no enzymatic PAS domain has been found. Here we report characterization of the first PAS enzyme: a haem-dependent oxidative N-demethylase. Unrelated to other amine oxidases, this enzyme contains haem, flavin mononucleotide, 2Fe-2S and tetrahydrofolic acid cofactors, and specifically catalyses the NADPH-dependent oxidation of dimethylamine. The structure of the alpha subunit reveals that it is a haem-binding PAS domain, similar in structure to PAS gas sensors. The dimethylamine substrate forms part of a highly polarized oxygen-binding site, and directly assists oxygen activation by acting as both an electron and proton donor. Our data reveal that the ubiquitous PAS domain can make the transition from sensor to enzyme, suggesting that the PAS scaffold can support the development of artificial enzymes.

An oxidative N-demethylase reveals PAS transition from ubiquitous sensor to enzyme.,Ortmayer M, Lafite P, Menon BR, Tralau T, Fisher K, Denkhaus L, Scrutton NS, Rigby SE, Munro AW, Hay S, Leys D Nature. 2016 Nov 24;539(7630):593-597. doi: 10.1038/nature20159. Epub 2016 Nov, 16. PMID:27851736<ref>PMID:27851736</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lth" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas mendocina]]
[[Category: Leys D]]
[[Category: Ortmayer M]]