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Instruments / Technical Area	Publication Details	Published	Actions
I04-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography	Structural basis of carnitine monooxygenase CntA substrate specificity, inhibition and inter-subunit electron transfer Mussa Quareshy , Muralidharan Shanmugam , Eleanor Townsend , Eleanor Jameson , Timothy D. H. Bugg , Alexander D. Cameron , Yin Chen Journal Of Biological Chemistry DOI: 10.1074/jbc.RA120.016019 Diamond Proposal Number(s): [19880] Show Abstract ▼ Abstract: Microbial metabolism of carnitine to trimethylamine (TMA) in the gut can accelerate atherosclerosis and heart disease and these TMA-producing enzymes are therefore important drug targets. Here, we report the first structures of the carnitine oxygenase CntA, an enzyme of the Rieske oxygenase family. CntA exists in a head-to-tail a3 trimeric structure. The two functional domains (the Rieske and the catalytic mononuclear iron domains) are located > 40 Å apart in the same monomer but adjacent in two neighbouring monomers. Structural determination of CntA and subsequent electron paramagnetic resonance measurements uncover the molecular basis of the so-called bridging glutamate (E205) residue in inter-subunit electron transfer. The structures of the substrate-bound CntA help to define the substrate pocket. Importantly, a tyrosine residue (Y203) is essential for ligand recognition through a π-cation interaction with the quaternary ammonium group. This interaction between an aromatic residue and quaternary amine substrates allows us to delineate a subgroup of Rieske oxygenases (group V) from the prototype ring-hydroxylating Rieske oxygenases involved in bioremediation of aromatic pollutants in the environment. Furthermore, we report the discovery of the first known CntA inhibitors and solve the structure of CntA in complex with the inhibitor, demonstrating the pivotal role of Y203 through a π-π stacking interaction with the inhibitor. Our study provides the structural and molecular basis for future discovery of drugs targeting this TMA-producing enzyme in human gut.	Nov 2020
I07-Surface & interface diffraction	Concentration-dependent adsorption of CsI at the muscovite - electrolyte interface Sander J. T. Brugman , Eleanor R. Townsend , Mireille M. H. Smets , Paolo Accordini , Elias Vlieg Langmuir DOI: 10.1021/acs.langmuir.8b00038 Diamond Proposal Number(s): [15042] Open Access Show Abstract ▼ Abstract: The interfacial structure of muscovite in contact with aqueous CsI solutions was measured using surface X-ray diffraction for several CsI concentrations (2 - 1000 mM). At CsI concentrations up to 200 mM, Cs+ adsorption is likely hindered by H3O+, as both cations compete for the adsorption site above the muscovite hexagonal cavity. Above this concentration, more Cs+ adsorbs than is required to compensate the negatively charged muscovite surface, which means that co-adsorption of an anion takes place. The I− anion does not co-adsorb in an ordered manner. Moreover, the hydration ring and water layers do not change significantly as function of CsI concentration.	Mar 2018

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