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The symptoms of diphtheria are due to an exotoxin that blocks proteins synthesis in host cells. The above statement is true.

The diphtheria toxin, also referred to as an A-B toxin, is a single polypeptide chain with 535 amino acids that is made up of two subunits connected by disulfide bridges. The B subunit, the less stable of the two subunits, binds to the cell surface, allowing the A subunit, the more stable portion of the protein, to enter the host cell. The crystal structure of the diphtheria toxin homodimer has been established to 2.5 Ångstrom resolution. Three domains make up the Y-shaped molecule that is revealed by the structure. The catalytic C domain is present in fragment A, while the T and R domains are present in fragment B.

The C domain, which is the amino-terminal catalytic domain, features a unique beta+alpha fold. By transferring ADP-ribose from NAD to a diphthamide residue of eukaryotic elongation factor, the C domain inhibits protein synthesis. The T domain or TM domain, a central translocation domain, lacks the first globin helix homologue but contains two extra helices at the amino terminus and a multi-helical globin-like fold. It is believed that this domain unfolds in the membrane. The transfer of the C domain into the cytoplasm and insertion into the endosomal membrane are both facilitated by a pH-induced conformational shift in the T domain.

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