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| | <StructureSection load='6u7i' size='340' side='right'caption='[[6u7i]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='6u7i' size='340' side='right'caption='[[6u7i]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6u7i]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_mucosus_anaerobius"_prausnitz_1922 "bacillus mucosus anaerobius" prausnitz 1922]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6U7I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6u7i]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Faecalibacterium_prausnitzii Faecalibacterium prausnitzii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6U7I FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CGS54_08875 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=853 "Bacillus mucosus anaerobius" Prausnitz 1922])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=6u7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u7i OCA], [https://pdbe.org/6u7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6u7i RCSB], [https://www.ebi.ac.uk/pdbsum/6u7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6u7i ProSAT]</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=6u7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u7i OCA], [https://pdbe.org/6u7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6u7i RCSB], [https://www.ebi.ac.uk/pdbsum/6u7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6u7i ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A3F3JX71_9FIRM A0A3F3JX71_9FIRM] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6u7i" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6u7i" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Galactosidase 3D structures|Galactosidase 3D structures]] |
| | + | *[[Glucuronisidase 3D structures|Glucuronisidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus mucosus anaerobius prausnitz 1922]] | + | [[Category: Faecalibacterium prausnitzii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ervin, S M]] | + | [[Category: Ervin SM]] |
| - | [[Category: Redinbo, M R]] | + | [[Category: Redinbo MR]] |
| - | [[Category: Glycosyl hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Microbiome]]
| + | |
| Structural highlights
Function
A0A3F3JX71_9FIRM
Publication Abstract from PubMed
Gut microbial beta-glucuronidase (GUS) enzymes have been suggested to be involved in the estrobolome, the collection of microbial reactions involving estrogens. Furthermore, bacterial GUS enzymes within the gastrointestinal tract have been postulated to be a contributing factor in hormone-driven cancers. However, to date, there has been no experimental evidence to support these hypotheses. Here we provide the first in vitro analysis of the ability of 35 human gut microbial GUS enzymes to reactivate two distinct estrogen glucuronides, estrone-3-glucuronide and estradiol-17-glucuronide, to estrone and estradiol, respectively. We show that certain members within the Loop 1, mini-Loop 1, and FMN-binding classes of gut microbial GUS enzymes can reactivate estrogens from their inactive glucuronides. We provide molecular details of key interactions that facilitate these catalytic processes and present the structures of two novel human gut microbial GUS enzymes related to the estrobolome. Further, we demonstrate that estrogen reactivation by Loop 1 bacterial GUS enzymes can be inhibited both in purified enzymes and in fecal preparations of mixed murine fecal microbiota. Finally, however, despite these in vitro and ex vivo data, we show that a Loop 1 GUS-specific inhibitor is not capable of reducing the development of tumors in the PyMT mouse model of breast cancer. These findings validate that gut microbial GUS enzymes participate in the estrobolome but also suggest that the estrobolome is a multidimensional set of processes on-going within the mammalian gastrointestinal tract that likely involves many enzymes, including several distinct types of GUS proteins.
Gut microbial beta-glucuronidases reactivate estrogens as components of the estrobolome that reactivate estrogens.,Ervin SM, Li H, Lim L, Roberts LR, Liang X, Mani S, Redinbo MR J Biol Chem. 2019 Dec 6;294(49):18586-18599. doi: 10.1074/jbc.RA119.010950. Epub , 2019 Oct 21. PMID:31636122[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ervin SM, Li H, Lim L, Roberts LR, Liang X, Mani S, Redinbo MR. Gut microbial beta-glucuronidases reactivate estrogens as components of the estrobolome that reactivate estrogens. J Biol Chem. 2019 Dec 6;294(49):18586-18599. doi: 10.1074/jbc.RA119.010950. Epub , 2019 Oct 21. PMID:31636122 doi:http://dx.doi.org/10.1074/jbc.RA119.010950
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