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Instruments / Technical Area	Publication Details	Published
Krios I-Titan Krios I at Diamond	Cryo-EM structures show the mechanistic basis of pan-peptidase inhibition by human α2-macroglobulin Daniel Luque , Theodoros Goulas , Carlos P. Mata , Soraia Mendes , F. Xavier Gomis-Rüth , Jose R. Caston Proceedings Of The National Academy Of Sciences 119 DOI: 10.1073/pnas.2200102119 Diamond Proposal Number(s): [2154] Show Abstract ▼ Abstract: Human α2-macroglobulin (hα2M) is a multidomain protein with a plethora of essential functions, including transport of signaling molecules and endopeptidase inhibition in innate immunity. Here, we dissected the molecular mechanism of the inhibitory function of the ∼720-kDa hα2M tetramer through eight cryo–electron microscopy (cryo-EM) structures of complexes from human plasma. In the native complex, the hα2M subunits are organized in two flexible modules in expanded conformation, which enclose a highly porous cavity in which the proteolytic activity of circulating plasma proteins is tested. Cleavage of bait regions exposed inside the cavity triggers rearrangement to a compact conformation, which closes openings and entraps the prey proteinase. After the expanded-to-compact transition, which occurs independently in the four subunits, the reactive thioester bond triggers covalent linking of the proteinase, and the receptor-binding domain is exposed on the tetramer surface for receptor-mediated clearance from circulation. These results depict the molecular mechanism of a unique suicidal inhibitory trap.	May 2022
I02-Macromolecular Crystallography	Structure of the receptor-binding carboxy-terminal domain of the bacteriophage T5 L-shaped tail fibre with and without its intra-molecular chaperone Carmela Garcia-Doval , José Castón , Daniel Luque , Meritxell Granell , José Otero , Antonio Llamas-Saiz , Madalena Renouard , Pascale Boulanger , Mark Van Raaij Viruses 7, 6424 - 6440 DOI: 10.3390/v7122946 PMID: 26670244 Diamond Proposal Number(s): [3808] Open Access Show Abstract ▼ Abstract: Bacteriophage T5, a Siphovirus belonging to the order Caudovirales, has a flexible, three-fold symmetric tail, to which three L-shaped fibres are attached. These fibres recognize oligo-mannose units on the bacterial cell surface prior to infection and are composed of homotrimers of the pb1 protein. Pb1 has 1396 amino acids, of which the carboxy-terminal 133 residues form a trimeric intra-molecular chaperone that is auto-proteolyzed after correct folding. The structure of a trimer of residues 970-1263 was determined by single anomalous dispersion phasing using incorporated selenomethionine residues and refined at 2.3 angstrom resolution using crystals grown from native, methionine-containing, protein. The protein inhibits phage infection by competition. The phage-distal receptor-binding domain resembles a bullet, with the walls formed by partially intertwined beta-sheets, conferring stability to the structure. The fold of the domain is novel and the topology unique to the pb1 structure. A site-directed mutant (Ser1264 to Ala), in which auto-proteolysis is impeded, was also produced, crystallized and its 2.5 angstrom structure solved by molecular replacement. The additional chaperone domain (residues 1263-1396) consists of a central trimeric alpha-helical coiled-coil flanked by a mixed alpha-beta domain. Three long beta-hairpin tentacles, one from each chaperone monomer, extend into long curved grooves of the bullet-shaped domain. The chaperone-containing mutant did not inhibit infection by competition.	Dec 2015
I02-Macromolecular Crystallography	Crystallization of the C-terminal domain of the bacteriophage T5 L-shaped fibre Mark Van Raaij , Carmela Garcia-Doval , Jose. R. Caston , Pascale Boulanger , Daniel Luque Acta Crystallographica F 69 (12), 1363–1367 DOI: 10.1107/S1744309113028959 PMID: 24316831 Diamond Proposal Number(s): [3808] Show Abstract ▼ Abstract: Tails of bacteriophage T5 (a member of the Siphoviridae family) were studied by electron microscopy. For the distal parts of the L-shaped tail fibres, which are involved in host cell receptor binding, a low-resolution volume was calculated. Several C-terminal fragments of the fibre were expressed and purified. Crystals of two of them were obtained that belonged to space groups P63 and R32 and diffracted synchrotron radiation to 2.3 and 2.9 A ° resolution, respectively. A single-wavelength anomalous dispersion data set to 2.5 A ° resolution was also collected from a selenomethionine-derivatized crystal of one of the fragments, which belonged to space group C2.	Dec 2013

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