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Instruments / Technical Area	Publication Details	Published
Krios III-Titan Krios III at Diamond	The structure of human thyroglobulin Francesca Coscia , Ajda Taler-Verčič , Veronica T. Chang , Ludwig Sinn , Francis J. O'Reilly , Thierry Izore , Miha Renko , Imre Berger , Juri Rappsilber , Dušan Turk , Jan Lowe Nature 37 DOI: 10.1038/s41586-020-1995-4 Diamond Proposal Number(s): [17434] Show Abstract ▼ Abstract: Thyroglobulin (TG) is the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates. Hormone synthesis from TG occurs in the thyroid gland via the iodination and coupling of pairs of tyrosines, and is completed by TG proteolysis3. Tyrosine proximity within TG is thought to enable the coupling reaction but hormonogenic tyrosines have not been clearly identified, and the lack of a three-dimensional structure of TG has prevented mechanistic understanding4. Here we present the structure of full-length human thyroglobulin at a resolution of approximately 3.5 Å, determined by cryo-electron microscopy. We identified all of the hormonogenic tyrosine pairs in the structure, and verified them using site-directed mutagenesis and in vitro hormone-production assays using human TG expressed in HEK293T cells. Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites. We transferred the reaction sites from TG to an engineered tyrosine donor–acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG. Our study provides a framework to further understand the production and regulation of thyroid hormones.	Feb 2020
I04-1-Macromolecular Crystallography (fixed wavelength) I04-Macromolecular Crystallography	Crenactin forms actin-like double helical filaments regulated by arcadin-2 Thierry Izore , Danguole Kureisaite-Ciziene , Stephen H Mclaughlin , Jan Lowe Elife 5 DOI: 10.7554/eLife.21600 Diamond Proposal Number(s): [11235] Open Access Show Abstract ▼ Abstract: The similarity of eukaryotic actin to crenactin, a filament-forming protein from the crenarchaeon Pyrobaculum calidifontis supports the theory of a common origin of Crenarchaea and Eukaryotes. Monomeric structures of crenactin and actin are similar, although their filament architectures were suggested to be different. Here we report that crenactin forms bona fide double helical filaments that show exceptional similarity to eukaryotic F-actin. With cryo-electron microscopy and helical reconstruction we solved the structure of the crenactin filament to 3.8 Å resolution. When forming double filaments, the 'hydrophobic plug' loop in crenactin rearranges. Arcadin-2, also encoded by the arcade gene cluster, binds tightly with its C-terminus to the hydrophobic groove of crenactin. Binding is reminiscent of eukaryotic actin modulators such as cofilin and thymosin β4 and arcadin-2 is a depolymeriser of crenactin filaments. Our work further supports the theory of shared ancestry of Eukaryotes and Crenarchaea.	Nov 2016
I24-Microfocus Macromolecular Crystallography	Structure of the tubulin/FtsZ-like protein TubZ from Pseudomonas bacteriophage ΦKZ Christopher Aylett , Thierry Izore , Linda Amos , Jan Lowe Journal Of Molecular Biology 425 (12), 2164 - 2173 DOI: 10.1016/j.jmb.2013.03.019 PMID: 23528827 Diamond Proposal Number(s): [8547] Open Access Show Abstract ▼ Abstract: Pseudomonas ΦKZ-like bacteriophages encode a group of related tubulin/FtsZ-like proteins believed to be essential for the correct centring of replicated bacteriophage virions within the bacterial host. In this study, we present crystal structures of the tubulin/FtsZ-like protein TubZ from Pseudomonas bacteriophage ΦKZ in both the monomeric and protofilament states, revealing that ΦKZ TubZ undergoes structural changes required to polymerise, forming a canonical tubulin/FtsZ-like protofilament. Combining our structures with previous work, we propose a polymerisation–depolymerisation cycle for the Pseudomonas bacteriophage subgroup of tubulin/FtsZ-like proteins. Electron cryo-microscopy of ΦKZ TubZ filaments polymerised in vitro implies a long-pitch helical arrangement for the constituent protofilaments. Intriguingly, this feature is shared by the other known subgroup of bacteriophage tubulin/FtsZ-like proteins from Clostridium species, which are thought to be involved in partitioning the genomes of bacteriophages adopting a pseudo-lysogenic life cycle.	Mar 2013

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