Figure 3.
FIG. 3. Analysis of lack of chloramphenicol sensitivity of
AfaE-III. a, backbone representations of the x-ray structures of
DraE (cyan) and AfaE-III (green) monomers as in Fig. 1b. The
-carbon positions of
the three amino acids that are altered between these different
strains are highlighted as numbered space filling balls. The
chloramphenicol bound to the DraE is shown in a ball-and-stick
representation and labeled Cm. b, analogous view of AfaE-III to
that shown of DraE in Fig. 2a. The residues that differ between
these adhesins are colored red. The side chain of Met-88 is seen
to lie across the Cm-binding pocket. c, Cm sensitivity of CD55
binding assayed by surface plasmon resonance (see "Experimental
Procedures"). Shown is CD55 (1 µM) binding to AfaE-III and
DraE in the absence (-) and presence (+) of Cm (2.8 mM). Values
presented are the mean and associated errors derived from three
(DraE) and six (AfaE-III) repeated measurements.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2004,
279,
46851-46857)
copyright 2004.
-carbon positions of
the three amino acids that are altered between these different
strains are highlighted as numbered space filling balls. The
chloramphenicol bound to the DraE is shown in a ball-and-stick
representation and labeled Cm. b, analogous view of AfaE-III to
that shown of DraE in Fig. 2a. The residues that differ between
these adhesins are colored red. The side chain of Met-88 is seen
to lie across the Cm-binding pocket. c, Cm sensitivity of CD55
binding assayed by surface plasmon resonance (see "Experimental
Procedures"). Shown is CD55 (1 µM) binding to AfaE-III and
DraE in the absence (-) and presence (+) of Cm (2.8 mM). Values
presented are the mean and associated errors derived from three
(DraE) and six (AfaE-III) repeated measurements.