The crystal structure of diphtheria toxin.

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.

journal_name

Nature

journal_title

Nature

authors

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

doi

10.1038/357216a0

keywords:

subject

Has Abstract

pub_date

1992-05-21 00:00:00

pages

216-22

issue

6375

eissn

0028-0836

issn

1476-4687

journal_volume

357

pub_type

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