4wkg

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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=4wkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wkg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wkg RCSB], [http://www.ebi.ac.uk/pdbsum/4wkg 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=4wkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wkg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wkg RCSB], [http://www.ebi.ac.uk/pdbsum/4wkg PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/ARNA_ECOLI ARNA_ECOLI]] Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.<ref>PMID:11706007</ref> <ref>PMID:15695810</ref>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 17:24, 25 December 2014

The crystal structure of apo ArnA features an unexpected central binding pocket and provides an explanation for enzymatic coop-erativity

4wkg, resolution 2.70Å

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