7cx1
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of a tyrosine decarboxylase from Enterococcus faecalis in complex with the cofactor PLP and inhibitor methyl-tyrosine== | |
- | + | <StructureSection load='7cx1' size='340' side='right'caption='[[7cx1]], [[Resolution|resolution]] 2.54Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[7cx1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CX1 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]] 2.54Å</td></tr> | |
- | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GKU:4-[(2R)-2-(methylamino)propyl]phenol'>GKU</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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=7cx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cx1 OCA], [https://pdbe.org/7cx1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cx1 RCSB], [https://www.ebi.ac.uk/pdbsum/7cx1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cx1 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/TYRDC_ENTFA TYRDC_ENTFA] Catalyzes the decarboxylation of L-tyrosine to produce tyramine (PubMed:30659181). Plays a role in acid resistance since tyramine production via tyrosine decarboxylation appears to provide a cytosolic pH maintenance mechanism that helps the bacterium cope with acid stress such as that encountered in gastrointestinal tract (GIT) environments. Therefore, may contribute to the colonization of the human GIT by E.faecalis (PubMed:25529314).<ref>PMID:25529314</ref> <ref>PMID:30659181</ref> Also involved in drug metabolism, being able to catalyze decarboxylation of levodopa (L-dopa) to dopamine. In gut microbiota this enzyme is in fact exclusively responsible for the decarboxylation of levodopa, and thus reduces in situ levels of levodopa in the treatment of Parkinson's disease. It was shown that abundance of bacterial tyrosine decarboxylase in the proximal small intestine - the primary site of levodopa absorption - contributes to interindividual variation in drug efficacy and can explain the requirement for an increased dosage regimen of levodopa treatment in Parkinson's disease patients.<ref>PMID:30659181</ref> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Enterococcus faecalis]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Chen C]] | ||
+ | [[Category: Gong M]] | ||
+ | [[Category: Guo R]] | ||
+ | [[Category: Huang J]] | ||
+ | [[Category: Liu W]] | ||
+ | [[Category: Yu X]] |
Current revision
Crystal structure of a tyrosine decarboxylase from Enterococcus faecalis in complex with the cofactor PLP and inhibitor methyl-tyrosine
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Categories: Enterococcus faecalis | Large Structures | Chen C | Gong M | Guo R | Huang J | Liu W | Yu X