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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography I04-Macromolecular Crystallography	Bacterial divisome protein FtsA forms curved antiparallel double filaments when binding to FtsN Tim Nierhaus , Stephen H. Mclaughlin , Frank Bürmann , Danguole Kureisaite-Ciziene , Sarah L. Maslen , J. Mark Skehel , Conny W. H. Yu , Stefan M. V. Freund , Louise F. H. Funke , Jason W. Chin , Jan Lowe Nature Microbiology 10 DOI: 10.1038/s41564-022-01206-9 Diamond Proposal Number(s): [15916, 21426] Show Abstract ▼ Abstract: During bacterial cell division, filaments of tubulin-like FtsZ form the Z-ring, which is the cytoplasmic scaffold for divisome assembly. In Escherichia coli, the actin homologue FtsA anchors the Z-ring to the membrane and recruits divisome components, including bitopic FtsN. FtsN regulates the periplasmic peptidoglycan synthase FtsWI. To characterize how FtsA regulates FtsN, we applied electron microscopy to show that E. coli FtsA forms antiparallel double filaments on lipid monolayers when bound to the cytoplasmic tail of FtsN. Using X-ray crystallography, we demonstrate that Vibrio maritimus FtsA crystallizes as an equivalent double filament. We identified an FtsA–FtsN interaction site in the IA–IC interdomain cleft of FtsA using X-ray crystallography and confirmed that FtsA forms double filaments in vivo by site-specific cysteine cross-linking. FtsA–FtsN double filaments reconstituted in or on liposomes prefer negative Gaussian curvature, like those of MreB, the actin-like protein of the elongasome. We propose that curved antiparallel FtsA double filaments together with treadmilling FtsZ filaments organize septal peptidoglycan synthesis in the division plane.	Sep 2022
I04-Macromolecular Crystallography I23-Long wavelength MX	Molecular mechanism of Mad1 kinetochore targeting by phosphorylated Bub1 Elyse S. Fischer , Conny W. H. Yu , Dom Bellini , Stephen H. Mclaughlin , Christian Orr , Armin Wagner , Stefan M. V. Freund , David Barford Embo Reports 536 DOI: 10.15252/embr.202052242 Open Access Show Abstract ▼ Abstract: During metaphase, in response to improper kinetochore-microtubule attachments, the spindle assembly checkpoint (SAC) activates the mitotic checkpoint complex (MCC), an inhibitor of the anaphase-promoting complex/cyclosome (APC/C). This process is orchestrated by the kinase Mps1, which initiates the assembly of the MCC onto kinetochores through a sequential phosphorylation-dependent signalling cascade. The Mad1-Mad2 complex, which is required to catalyse MCC formation, is targeted to kinetochores through a direct interaction with the phosphorylated conserved domain 1 (CD1) of Bub1. Here, we present the crystal structure of the C-terminal domain of Mad1 (Mad1CTD) bound to two phosphorylated Bub1CD1 peptides at 1.75 Å resolution. This interaction is mediated by phosphorylated Bub1 Thr461, which not only directly interacts with Arg617 of the Mad1 RLK (Arg-Leu-Lys) motif, but also directly acts as an N-terminal cap to the CD1 α-helix dipole. Surprisingly, only one Bub1CD1 peptide binds to the Mad1 homodimer in solution. We suggest that this stoichiometry is due to inherent asymmetry in the coiled-coil of Mad1CTD and has implications for how the Mad1-Bub1 complex at kinetochores promotes efficient MCC assembly.	May 2021

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