Crystal structure and functional characterization of SF216 from Shigella flexneri

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.

Complete genome sequence and annotation of the laboratory reference strain Shigella flexneri serotype 5a M90T and genome-wide transcriptional start site determination

“…S. flexneri 5a M90T, along with S. flexneri 2a, is one of the most commonly employed laboratory reference strain for S. flexneri in many independent research groups across the globe [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27]. Indeed, much of our knowledge of the molecular mechanisms of Shigella pathogenesis has been obtained using S. flexneri M90T as a model.…”