Nature. 1992 May 21;357(6375):216-22.

The crystal structure of diphtheria toxin.

Choe S, Bennett MJ, Fujii G, Curmi PM, Kantardjieff KA, Collier RJ, Eisenberg D.

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Department of Chemistry and Biochemistry, University of California, Los Angeles 90024.

Abstract

The crystal structure of the diphtheria toxin dimer at 2.5 A resolution reveals a Y-shaped molecule of three domains. The catalytic domain, called fragment A, is of the alpha + beta type. Fragment B actually consists of two domains. The transmembrane domain consists of nine alpha-helices, two pairs of which are unusually apolar and may participate in pH-triggered membrane insertion and translocation. The receptor-binding domain is a flattened beta-barrel with a jelly-roll-like topology. Three distinct functions of the toxin, each carried out by a separate structural domain, can be useful in designing chimaeric proteins, such as immunotoxins, in which the receptor-binding domain is substituted with antibodies to target other cell types.

PMID:: 1589020; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Nucleotide-Free Diphtheria Toxinÿ

PDB: 1SGK

Source: Corynephage beta

Method: X-Ray Diffraction

Resolution: 2.3 Å

See all 4 structures...

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