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J. Biol. Chem., Vol. 276, Issue 29, 27535-27540, July 20, 2001
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§,
, and
From the The TonB-dependent complex of
Gram-negative bacteria couples the inner membrane proton motive force
to the active transport of iron·siderophore and vitamin
B12 across the outer membrane. The structural basis
of that process has not been described so far in full detail. The
crystal structure of the C-terminal domain of TonB from
Escherichia coli has now been solved by multiwavelength anomalous diffraction and refined at 1.55-Å resolution, providing the
first evidence that this region of TonB (residues 164-239) dimerizes.
Moreover, the structure shows a novel architecture that has no
structural homologs among any known proteins. The dimer of the
C-terminal domain of TonB is cylinder-shaped with a length of 65 Å and
a diameter of 25 Å. Each monomer contains three
Macromolecular Crystallography Laboratory,
NCI, National Institutes of Health, Frederick, Maryland 21702 and the
¶ Biochemisches Institut der Universität Zürich,
Winterthurerstrasse 190, Zürich CH-8057, Switzerland
strands and a
single
helix. The two monomers are intertwined with each other, and
all six
-strands of the dimer make a large antiparallel
-sheet.
We propose a plausible model of binding of TonB to FhuA and FepA, two
TonB-dependent outer-membrane receptors.
To whom correspondence should be addressed: Biochemisches
Institut der Universität Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland. Tel.: 41-1-635-5570; Fax:
41-1-635-5712; E-mail: plueckthun@biocfebs.unizh.ch.
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