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• W2762798049 abstract "Shigella flexneri is a Gram-negative anaerobic bacterium that causes highly infectious bacterial dysentery in humans. Here, we solved the crystal structure of SF216, a hypothetical protein from the S. flexneri 5a strain M90T, at 1.7 Å resolution. The crystal structure of SF216 represents a homotrimer stabilized by intersubunit interactions and ion-mediated electrostatic interactions. Each subunit consists of three β-strands and five α-helices with the β-β-β-α-α-α-α-α topology. Based on the structural information, we also demonstrate that SF216 shows weak ribonuclease activity by a fluorescence quenching assay. Furthermore, we identify potential druggable pockets (putative hot spots) on the surface of the SF216 structure by computational mapping." @default.
• W2762798049 created "2017-10-20" @default.
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• W2762798049 date "2017-10-17" @default.
• W2762798049 modified "2023-10-17" @default.
• W2762798049 title "Crystal structure and functional characterization of SF216 from Shigella flexneri" @default.
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• W2762798049 doi "https://doi.org/10.1002/1873-3468.12873" @default.
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