View source for 3weu


==Crystal structure of the L-Lys epsilon-oxidase from Marinomonas mediterranea==
<StructureSection load='3weu' size='340' side='right'caption='[[3weu]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3weu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Marm1 Marm1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WEU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wev|3wev]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lodA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=717774 MARM1])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/L-lysine_6-oxidase L-lysine 6-oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.20 1.4.3.20] </span></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=3weu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3weu OCA], [https://pdbe.org/3weu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3weu RCSB], [https://www.ebi.ac.uk/pdbsum/3weu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3weu ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/LODA_MARM1 LODA_MARM1]] Has antibacterial activity against a wide spectrum of Gram-positive and Gram-negative bacteria including nosocomial isolates of S.aureus and Pseudomonas sp. The antimicrobial activity is due to hydrogen peroxide generated by its lysine oxidase activity. Also has autotoxic activity. Involved in biofilm differentiation; responsible for cell death within microcolonies during biofilm development which is linked to the generation of a phenotypically diverse dispersal population and thus may play a role in colonization.<ref>PMID:15652194</ref> <ref>PMID:18502869</ref> <ref>PMID:20025674</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have determined the x-ray crystal structure of l-lysine epsilon-oxidase from Marinomonas mediterranea in its native and l-lysine-complex forms at 1.94- and 1.99-A resolution, respectively. In the native enzyme, electron densities clearly indicate the presence of cysteine tryptophylquinone (CTQ) previously identified in quinohemoprotein amine dehydrogenase. In the l-lysine-complex, an electron density corresponding to the bound l-lysine shows that its epsilon-amino group is attached to the C6 carbonyl group of CTQ, suggesting the formation of a Schiff-base intermediate. Collectively, the present crystal structure provides the first example of an enzyme employing a tryptophylquinone cofactor in an amine oxidase.

X-Ray crystallographic evidence for the presence of the cysteine tryptophylquinone cofactor in L-lysine {varepsilon}-oxidase from Marinomonas mediterranea.,Okazaki S, Nakano S, Matsui D, Akaji S, Inagaki K, Asano Y J Biochem. 2013 Sep;154(3):233-6. doi: 10.1093/jb/mvt070. Epub 2013 Aug 1. PMID:23908359<ref>PMID:23908359</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3weu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: L-lysine 6-oxidase]]
[[Category: Large Structures]]
[[Category: Marm1]]
[[Category: Akaji, S]]
[[Category: Asano, Y]]
[[Category: Inagaki, K]]
[[Category: Matsui, D]]
[[Category: Nakano, S]]
[[Category: Okazaki, S]]
[[Category: Amine oxidase]]
[[Category: Amino acid oxidase]]
[[Category: Arm]]
[[Category: Beta barrel]]
[[Category: L-lys binding]]
[[Category: Oxidoreductase]]
[[Category: Three beta sheet]]