5UJ6

Crystal Structure of Bacteroides Uniformis beta-glucuronidase

Summary for 5UJ6

• Entry DOI: 10.2210/pdb5uj6/pdb
• Descriptor: Glycosyl hydrolases family 2, sugar binding domain protein, GLYCEROL, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: glucuronic-acid carbohydrate, hydrolase
• Biological source: Bacteroides uniformis str. 3978 T3 ii
• Total number of polymer chains: 2
• Total formula weight: 201741.34

Authors

Walton, W.G.,Redinbo, M.R. (deposition date: 2017-01-17, release date: 2017-06-28, Last modification date: 2024-03-06)

Primary citation

Pollet, R.M.,D'Agostino, E.H.,Walton, W.G.,Xu, Y.,Little, M.S.,Biernat, K.A.,Pellock, S.J.,Patterson, L.M.,Creekmore, B.C.,Isenberg, H.N.,Bahethi, R.R.,Bhatt, A.P.,Liu, J.,Gharaibeh, R.Z.,Redinbo, M.R.
An Atlas of beta-Glucuronidases in the Human Intestinal Microbiome.
Structure, 25:967-977.e5, 2017

PubMed Abstract: Microbiome-encoded β-glucuronidase (GUS) enzymes play important roles in human health by metabolizing drugs in the gastrointestinal (GI) tract. The numbers, types, and diversity of these proteins in the human GI microbiome, however, remain undefined. We present an atlas of GUS enzymes comprehensive for the Human Microbiome Project GI database. We identify 3,013 total and 279 unique microbiome-encoded GUS proteins clustered into six unique structural categories. We assign their taxonomy, assess cellular localization, reveal the inter-individual variability within the 139 individuals sampled, and discover 112 novel microbial GUS enzymes. A representative in vitro panel of the most common GUS proteins by read abundances highlights structural and functional variabilities within the family, including their differential processing of smaller glucuronides and larger carbohydrates. These data provide a sequencing-to-molecular roadmap for examining microbiome-encoded enzymes essential to human health.

PubMed: 28578872
DOI: 10.1016/j.str.2017.05.003

Experimental method

X-RAY DIFFRACTION (1.9 Å)