View source for 8po5


==Lactobacillus plantarum LpdD==
<StructureSection load='8po5' size='340' side='right'caption='[[8po5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8po5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus Lactobacillus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8PO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PO5 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=8po5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8po5 OCA], [https://pdbe.org/8po5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8po5 RCSB], [https://www.ebi.ac.uk/pdbsum/8po5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8po5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LPDD_LACPL LPDD_LACPL] Probably involved in tannin degradation, however the precise biochemical function in metabolism of gallate is unknown.<ref>PMID:23645198</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The UbiD enzyme family of prenylated flavin (prFMN)-dependent reversible decarboxylases is near ubiquitously present in microbes. For some UbiD family members, enzyme activation through prFMNH(2) binding and subsequent oxidative maturation of the cofactor readily occurs, both in vivo in a heterologous host and through in vitro reconstitution. However, isolation of the active holo-enzyme has proven intractable for others, notably the canonical Escherichia coli UbiD. We show that E. coli heterologous expression of the small protein LpdD-associated with the UbiD-like gallate decarboxylase LpdC from Lactobacillus plantarum-unexpectedly leads to 3,4-dihydroxybenzoic acid decarboxylation whole-cell activity. This activity was shown to be linked to endogenous E. coli ubiD expression levels. The crystal structure of the purified LpdD reveals a dimeric protein with structural similarity to the eukaryotic heterodimeric proteasome assembly chaperone Pba3/4. Solution studies demonstrate that LpdD protein specifically binds to reduced prFMN species only. The addition of the LpdD-prFMNH(2) complex supports reconstitution and activation of the purified E. coli apo-UbiD in vitro, leading to modest 3,4-dihydroxybenzoic acid decarboxylation. These observations suggest that LpdD acts as a prFMNH(2)-binding chaperone, enabling apo-UbiD activation through enhanced prFMNH(2) incorporation and subsequent oxidative maturation. Hence, while a single highly conserved flavin prenyltransferase UbiX is found associated with UbiD enzymes, our observations suggest considerable diversity in UbiD maturation, ranging from robust autocatalytic to chaperone-mediated processes. Unlocking the full (de)carboxylation scope of the UbiD-enzyme family will thus require more than UbiX coexpression.

The prFMNH(2)-binding chaperone LpdD assists UbiD decarboxylase activation.,Gahloth D, Fisher K, Marshall S, Leys D J Biol Chem. 2024 Feb;300(2):105653. doi: 10.1016/j.jbc.2024.105653. Epub 2024 , Jan 13. PMID:38224946<ref>PMID:38224946</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8po5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactobacillus]]
[[Category: Large Structures]]
[[Category: Gahloth D]]
[[Category: Leys D]]