View source for 6se3


==Crystal Structure of Ancestral Flavin-containing monooxygenase (FMO) 3-6==
<StructureSection load='6se3' size='340' side='right'caption='[[6se3]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6se3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SE3 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=6se3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6se3 OCA], [https://pdbe.org/6se3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6se3 RCSB], [https://www.ebi.ac.uk/pdbsum/6se3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6se3 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Flavin-containing monooxygenases (FMOs) are ubiquitous in all domains of life and metabolize a myriad of xenobiotics, including toxins, pesticides and drugs. However, despite their pharmacological importance, structural information remains bereft. To further our understanding behind their biochemistry and diversity, we used ancestral-sequence reconstruction, kinetic and crystallographic techniques to scrutinize three ancient mammalian FMOs: AncFMO2, AncFMO3-6 and AncFMO5. Remarkably, all AncFMOs could be crystallized and were structurally resolved between 2.7- and 3.2-A resolution. These crystal structures depict the unprecedented topology of mammalian FMOs. Each employs extensive membrane-binding features and intricate substrate-profiling tunnel networks through a conspicuous membrane-adhering insertion. Furthermore, a glutamate-histidine switch is speculated to induce the distinctive Baeyer-Villiger oxidation activity of FMO5. The AncFMOs exhibited catalysis akin to human FMOs and, with sequence identities between 82% and 92%, represent excellent models. Our study demonstrates the power of ancestral-sequence reconstruction as a strategy for the crystallization of proteins.

Ancestral-sequence reconstruction unveils the structural basis of function in mammalian FMOs.,Nicoll CR, Bailleul G, Fiorentini F, Mascotti ML, Fraaije MW, Mattevi A Nat Struct Mol Biol. 2019 Dec 23. pii: 10.1038/s41594-019-0347-2. doi:, 10.1038/s41594-019-0347-2. PMID:31873300<ref>PMID:31873300</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6se3" style="background-color:#fffaf0;"></div>

==See Also==
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Bailleul G]]
[[Category: Fiorentini F]]
[[Category: Fraaije M]]
[[Category: Mascotti ML]]
[[Category: Mattevi A]]
[[Category: Nicoll C]]