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2ymw

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ymw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ymw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ymw RCSB], [http://www.ebi.ac.uk/pdbsum/2ymw PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ymw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ymw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ymw RCSB], [http://www.ebi.ac.uk/pdbsum/2ymw PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://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>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 22:44, 25 December 2014

Structure of the epsilon-lysine oxidase from Marinomonas mediterranea

2ymw, resolution 2.41Å

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