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Diphtheria toxin

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== Function ==
== Function ==
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'''Diphtheria toxin''' (DT) is a toxin which is secreted by the bacteria causing diphtheria. DT contains 2 subunits. Subunit A contains the catalytic domain and subunit B contains the transmembrane and receptor-binding domains. DT catalyzes the transfer of NAD to a diphthamide residue in the elongatin factor-2 and thus inhibiting protein synthesis.
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'''Diphtheria toxin''' (DT) is a toxin which is secreted by the bacteria causing diphtheria. DT catalyzes the transfer of NAD to a diphthamide residue in the elongatin factor-2 and thus inhibiting protein synthesis.
== Disease ==
== Disease ==
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== Relevance ==
== Relevance ==
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DT is used in several drugs as chemotherapeutic agent and as an immunotoxin.
== Structural highlights ==
== Structural highlights ==
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DT is proteolitically cleaved into 2 fragments. Fragment A contains the catalytic domain (C) and fragment B contains the transmembrane (T) and receptor-binding (R) domains. DT active site is located in a cleft in the C domain.<ref>PMID:7833807</ref>
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</StructureSection>

Revision as of 12:15, 30 December 2015

Structure of diphtheria toxin complex with NAD (PDB code 1tox).

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3D structures of diphtheria toxin

Updated on 30-December-2015

References

  1. Bennett MJ, Choe S, Eisenberg D. Refined structure of dimeric diphtheria toxin at 2.0 A resolution. Protein Sci. 1994 Sep;3(9):1444-63. PMID:7833807

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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