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Instruments / Technical Area	Publication Details	Published
I24-Microfocus Macromolecular Crystallography	Structure and diffusive dynamics of Aspartate α-decarboxylase (ADC) liganded with D-Serine in aqueous solution Tushar Raskar , Stephan Niebling , Juliette M. Devos , Briony A. Yorke , Michael Haertlein , Nils Huse , V. Trevor Forsyth , Tilo Seydel , Arwen R. Pearson Physical Chemistry Chemical Physics DOI: 10.1039/D2CP02063G Diamond Proposal Number(s): [6386] Open Access Show Abstract ▼ Abstract: Incoherent neutron spectroscopy, in combination with dynamic light scattering, was used to investigate the effect of ligand binding on the center-of-mass self-diffusion and internal diffusive dynamics of Escherichia coli aspartate α-decarboxylase (ADC). The X-ray crystal structure of ADC in complex with the D-Serine inhibitor was also determined, and molecular dynamics simulations were used to further probe the structural rearrangements that occur as a result of ligand binding. These experiments reveal that D-Serine forms hydrogen bonds with some of the active site residues, that higher order oligomers of the ADC tetramer exist on ns-ms time-scales, and also show that ligand binding both affects the ADC internal diffusive dynamics and appears to further increase the size of the higher order oligomers.	Aug 2022
I04-1-Macromolecular Crystallography (fixed wavelength)	Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD Luke A. Perera , Steffen Preissler , Nathan R. Zaccai , Sylvain Prévost , Juliette M. Devos , Michael Haertlein , David Ron Nature Communications 12 DOI: 10.1038/s41467-021-25076-7 Diamond Proposal Number(s): [21426] Open Access Show Abstract ▼ Abstract: The endoplasmic reticulum (ER) Hsp70 chaperone BiP is regulated by AMPylation, a reversible inactivating post-translational modification. Both BiP AMPylation and deAMPylation are catalysed by a single ER-localised enzyme, FICD. Here we present crystallographic and solution structures of a deAMPylation Michaelis complex formed between mammalian AMPylated BiP and FICD. The latter, via its tetratricopeptide repeat domain, binds a surface that is specific to ATP-state Hsp70 chaperones, explaining the exquisite selectivity of FICD for BiP’s ATP-bound conformation both when AMPylating and deAMPylating Thr518. The eukaryotic deAMPylation mechanism thus revealed, rationalises the role of the conserved Fic domain Glu234 as a gatekeeper residue that both inhibits AMPylation and facilitates hydrolytic deAMPylation catalysed by dimeric FICD. These findings point to a monomerisation-induced increase in Glu234 flexibility as the basis of an oligomeric state-dependent switch between FICD’s antagonistic activities, despite a similar mode of engagement of its two substrates — unmodified and AMPylated BiP.	Aug 2021
B21-High Throughput SAXS	Molecular changes in dengue envelope protein domain III upon interaction with glycosaminoglycans James G. Hyatt , Sylvain Prévost , Juliette M. Devos , Courtney J. Mycroft-West , Mark A. Skidmore , Anja Winter Pathogens 9 DOI: 10.3390/pathogens9110935 Diamond Proposal Number(s): [25074] Open Access Show Abstract ▼ Abstract: Dengue fever is a rapidly emerging vector-borne viral disease with a growing global burden of approximately 390 million new infections per annum. The Dengue virus (DENV) is a flavivirus spread by female mosquitos of the aedes genus, but the mechanism of viral endocytosis is poorly understood at a molecular level, preventing the development of effective transmission blocking vaccines (TBVs). Recently, glycosaminoglycans (GAGs) have been identified as playing a role during initial viral attachment through interaction with the third domain of the viral envelope protein (EDIII). Here, we report a systematic study investigating the effect of a range of biologically relevant GAGs on the structure and oligomeric state of recombinantly generated EDIII. We provide novel in situ biophysical evidence that heparin and chondroitin sulphate C induce conformational changes in EDIII at the secondary structure level. Furthermore, we report the ability of chondroitin sulphate C to bind EDIII and induce higher-order dynamic molecular changes at the tertiary and quaternary structure levels which are dependent on pH, GAG species, and the GAG sulphation state. Lastly, we conducted ab initio modelling of Small Angle Neutron Scattering (SANS) data to visualise the induced oligomeric state of EDIII caused by interaction with chondroitin sulphate C, which may aid in TBV development.	Nov 2020
I04-Macromolecular Crystallography	Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme Hanna Kwon , Jaswir Basran , Cecilia M. Casadei , Alistair J. Fielding , Tobias E. Schrader , Andreas Ostermann , Juliette M. Devos , Pierre Aller , Matthew P. Blakeley , P. C. E. Moody , Emma L. Raven Nature Communications 7 DOI: 10.1038/ncomms13445 Diamond Proposal Number(s): [10369] Open Access Show Abstract ▼ Abstract: Catalytic heme enzymes carry out a wide range of oxidations in biology. They have in common a mechanism that requires formation of highly oxidized ferryl intermediates. It is these ferryl intermediates that provide the catalytic engine to drive the biological activity. Unravelling the nature of the ferryl species is of fundamental and widespread importance. The essential question is whether the ferryl is best described as a Fe(IV)=O or a Fe(IV)–OH species, but previous spectroscopic and X-ray crystallographic studies have not been able to unambiguously differentiate between the two species. Here we use a different approach. We report a neutron crystal structure of the ferryl intermediate in Compound II of a heme peroxidase; the structure allows the protonation states of the ferryl heme to be directly observed. This, together with pre-steady state kinetic analyses, electron paramagnetic resonance spectroscopy and single crystal X-ray fluorescence, identifies a Fe(IV)–OH species as the reactive intermediate. The structure establishes a precedent for the formation of Fe(IV)–OH in a peroxidase.	Nov 2016

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