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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography I04-Macromolecular Crystallography I23-Long wavelength MX	Functional metagenomic screening identifies an unexpected β-glucuronidase Stefanie Neun , Paul Brear , Eleanor Campbell , Theodora Tryfona , Kamel El Omari , Armin Wagner , Paul Dupree , Marko Hyvonen , Florian Hollfelder Nature Chemical Biology 48 DOI: 10.1038/s41589-022-01071-x Diamond Proposal Number(s): [18548, 25402] Show Abstract ▼ Abstract: The abundance of recorded protein sequence data stands in contrast to the small number of experimentally verified functional annotation. Here we screened a million-membered metagenomic library at ultrahigh throughput in microfluidic droplets for β-glucuronidase activity. We identified SN243, a genuine β-glucuronidase with little homology to previously studied enzymes of this type, as a glycoside hydrolase 3 family member. This glycoside hydrolase family contains only one recently added β-glucuronidase, showing that a functional metagenomic approach can shed light on assignments that are currently ‘unpredictable’ by bioinformatics. Kinetic analyses of SN243 characterized it as a promiscuous catalyst and structural analysis suggests regions of divergence from homologous glycoside hydrolase 3 members creating a wide-open active site. With a screening throughput of >107 library members per day, picolitre-volume microfluidic droplets enable functional assignments that complement current enzyme database dictionaries and provide bridgeheads for the annotation of unexplored sequence space.	Jul 2022
I02-Macromolecular Crystallography	Glycan complexity dictates microbial resource allocation in the large intestine Artur Rogowski , Jonathon A. Briggs , Jennifer C. Mortimer , Theodora Tryfona , Nicolas Terrapon , Elisabeth C. Lowe , Arnaud Baslé , Carl Morland , Alison M. Day , Hongjun Zheng , Theresa E. Rogers , Paul Thompson , Alastair R. Hawkins , Madhav P. Yadav , Bernard Henrissat , Eric C. Martens , Paul Dupree , Harry J. Gilbert , David N. Bolam Nature Communications 6, 7481 DOI: 10.1038/ncomms8481 PMID: 26112186 Open Access Show Abstract ▼ Abstract: The structure of the human gut microbiota is controlled primarily through the degradation of complex dietary carbohydrates, but the extent to which carbohydrate breakdown products are shared between members of the microbiota is unclear. We show here, using xylan as a model, that sharing the breakdown products of complex carbohydrates by key members of the microbiota, such as Bacteroides ovatus, is dependent on the complexity of the target glycan. Characterization of the extensive xylan degrading apparatus expressed by B. ovatus reveals that the breakdown of the polysaccharide by the human gut microbiota is significantly more complex than previous models suggested, which were based on the deconstruction of xylans containing limited monosaccharide side chains. Our report presents a highly complex and dynamic xylan degrading apparatus that is fine-tuned to recognize the different forms of the polysaccharide presented to the human gut microbiota.	Jun 2015

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