 |
|
Title
|
|
The crystal structure of diphtheria toxin.
|
|
|
Authors
|
|
S.Choe,
M.J.Bennett,
G.Fujii,
P.M.Curmi,
K.A.Kantardjieff,
R.J.Collier,
D.Eisenberg.
|
|
|
Ref.
|
|
Nature, 1992,
357,
216-222.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|