PROXIMA-1 beamline for macromolecular crystallography measurements at Synchrotron SOLEIL

Chavas, Leonard M. G.; Gourhant, Patrick; Guimarães, B.G.; Isabet, T.; Legrand, Pierre; Lener, Robin; Montaville, Pierre; Sirigu, Serena; Thompson, Andrew

doi:10.1107/s1600577521002605

Cited by 15 publications

(13 citation statements)

References 20 publications

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“…Diffraction data were collected on the PROXIMA-1 beamline at the synchrotron SOLEIL (Saint-Aubin, France) 52 . A crystal of holo-native Mmp10 with peptide substrate (Mmp10–SAM–peptide structure) belonging to the space group P 6 3 was detected, and diffraction data were collected to 2.4 Å with phases obtained through multiwavelength anomalous diffraction (MAD).…”

Section: Methodsmentioning

confidence: 99%

Crystallographic snapshots of a B12-dependent radical SAM methyltransferase

Fyfe

Bernardo-García

Fradale

et al. 2022

Nature

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By catalysing the microbial formation of methane, methyl-coenzyme M reductase has a central role in the global levels of this greenhouse gas1,2. The activity of methyl-coenzyme M reductase is profoundly affected by several unique post-translational modifications3–6, such as a unique C-methylation reaction catalysed by methanogenesis marker protein 10 (Mmp10), a radical S-adenosyl-l-methionine (SAM) enzyme7,8. Here we report the spectroscopic investigation and atomic resolution structure of Mmp10 from Methanosarcina acetivorans, a unique B12 (cobalamin)-dependent radical SAM enzyme9. The structure of Mmp10 reveals a unique enzyme architecture with four metallic centres and critical structural features involved in the control of catalysis. In addition, the structure of the enzyme–substrate complex offers a glimpse into a B12-dependent radical SAM enzyme in a precatalytic state. By combining electron paramagnetic resonance spectroscopy, structural biology and biochemistry, our study illuminates the mechanism by which the emerging superfamily of B12-dependent radical SAM enzymes catalyse chemically challenging alkylation reactions and identifies distinctive active site rearrangements to provide a structural rationale for the dual use of the SAM cofactor for radical and nucleophilic chemistry.

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Section: Methodsmentioning

confidence: 99%

Crystallographic snapshots of a B12-dependent radical SAM methyltransferase

Fyfe

Bernardo-García

Fradale

et al. 2022

Nature

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“…The native, the derivative (iodine-soaked) and the ‘glycosylated’ data were all collected at 100K on the Proxima-1 46 or Proxima-2A beamlines at the SOLEIL synchrotron source (Saint Aubin, France), using the Pilatus Eiger X 16M or Eiger X 9M detectors (Dectris), respectively.…”

Section: Methodsmentioning

confidence: 99%

The crystal structure of a simian Foamy Virus receptor binding domain provides clues about entry into host cells

Fernández

Dynesen

Coquin

et al. 2022

Preprint

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The surface envelope glycoprotein (Env) of all retroviruses mediates virus binding to cells and fusion of the viral and cellular membranes. A structure-function relationship for the HIV Env, which belongs to the Orthoretrovirus subfamily, has been well established. Structural information is however largely missing for the Env of Foamy viruses (FVs), the second retroviral subfamily. FV Envs lack sequence similarity with their HIV counterpart. We present the X-ray structure of the receptor binding domain (RBD) of a simian FV Env at 2.6 Å resolution, revealing two subdomains and an unprecedented fold. We have generated a model for the organization of the RBDs within the trimeric Env which indicates that the upper subdomain is important for stabilization of the full-length Env, and have demonstrated that residues K342, R343, R359 and R369 in the lower subdomain play key roles in the interaction of the RBD and viral particles with heparan sulfate.

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“…Diffraction data collection and refinement statistics are given in Supplementary table S1 . Crystallographic data were collected on the PROXIMA-1 (Chavas et al, 2021) beamlines at Synchrotron SOLEIL (Saint-Aubin, France) and processed with XDS (Kabsch, 2010) through XDSME (https://github.com/legrandp/xdsme) (Legrand, 2017). The strong diffraction anisotropy was corrected using the STARANISO program (Tickle et al, 2018).…”

Section: Materiel and Methodsmentioning

confidence: 99%

DNA-binding mechanism and evolution of Replication Protein A

Madru

Martínez‐Carranza

Laurent

et al. 2022

Preprint

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Replication Protein A (RPA) is a heterotrimeric single stranded DNA-binding protein with essential roles in DNA replication, recombination and repair, in both eukaryotic and archaeal cells. By using an integrative approach that combines three crystal structures, four cryo-EM structures in complex with single-stranded DNA (ssDNA) of different lengths, we extensively characterized RPA from Pyrococcus abyssi in different states. These structures show two essential features conserved in eukaryotes: a trimeric core and a module that promotes cooperative binding to ssDNA, as well as a newly identified archaeal-specific domain. These structures reveal for the first time how ssDNA is handed over from one RPA complex to the other, and uncover an unanticipated mechanism of self-association on ssDNA tracts. This work constitutes a significant step forward in the molecular understanding of the structure and DNA-binding mechanism of RPA, with far-reaching implications for the evolution of this primordial replication factor in Archaea and Eukarya.

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PROXIMA-1 beamline for macromolecular crystallography measurements at Synchrotron SOLEIL

Cited by 15 publications

References 20 publications

Crystallographic snapshots of a B12-dependent radical SAM methyltransferase

Crystallographic snapshots of a B12-dependent radical SAM methyltransferase

The crystal structure of a simian Foamy Virus receptor binding domain provides clues about entry into host cells

DNA-binding mechanism and evolution of Replication Protein A

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