ArticleProtein science : a publication of the Protein Society2018
Active site flexibility revealed in crystal structures of Parabacteroides merdae β-glucuronidase from the human gut microbiome.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.
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Who cites it
12 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.
- Gut microbiota-associated predictors as biomarkers of neoadjuvant treatment response in rectal cancer-a systematic review.British journal of cancer · 2026Pooled it
- The testobolome in microbial testosterone metabolism and human health.NPJ biofilms and microbiomes · 2026Review
- Catabolism ofFoods (Basel, Switzerland) · 2023Article
- Characterizing the metabolic effects of the selective inhibition of gut microbial β-glucuronidases in mice.Scientific reports · 2022Article
- Functional metagenomic screening identifies an unexpected β-glucuronidase.Nature chemical biology · 2022Article
- The role of gut microbial β-glucuronidase in drug disposition and development.Drug discovery today · 2022Review
- A structural metagenomics pipeline for examining the gut microbiome.Current opinion in structural biology · 2022Review
- Towards a 'chassis' for bacterial magnetosome biosynthesis: genome streamlining of Magnetospirillum gryphiswaldense by multiple deletions.Microbial cell factories · 2021Article
- Predicting drug-metagenome interactions: Variation in the microbial β-glucuronidase level in the human gut metagenomes.PloS one · 2021Article
- Targeted inhibition of gut bacterial β-glucuronidase activity enhances anticancer drug efficacy.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Gut microbial β-glucuronidases reactivate estrogens as components of the estrobolome that reactivate estrogens.The Journal of biological chemistry · 2019Article
- Selecting a Single Stereocenter: The Molecular Nuances That Differentiate β-Hexuronidases in the Human Gut Microbiome.Biochemistry · 2019Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
β-Glucuronidase (GUS) enzymes in the gastrointestinal tract are involved in maintaining mammalian-microbial symbiosis and can play key roles in drug efficacy and toxicity. Parabacteroides merdae GUS was identified as an abundant mini-Loop 2 (mL2) type GUS enzyme in the Human Microbiome Project gut metagenomic database. Here, we report the crystal structure of P. merdae GUS and highlight the differences between this enzyme and extant structures of gut microbial GUS proteins. We find that P. merdae GUS exhibits a distinct tetrameric quaternary structure and that the mL2 motif traces a unique path within the active site, which also includes two arginines distinctive to this GUS. We observe two states of the P. merdae GUS active site; a loop repositions itself by more than 50 Å to place a functionally-relevant residue into the enzyme's catalytic site. Finally, we find that P. merdae GUS is able to bind to homo and heteropolymers of the polysaccharide alginic acid. Together, these data broaden our understanding of the structural and functional diversity in the GUS family of enzymes present in the human gut microbiome and point to specialization as an important feature of microbial GUS orthologs.
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