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Figure 4.
Figure 4. Structural Comparisons of Three Peptides
Interacting with Helices H and I of the Apical DomainSBP is
yellow, the GroES mobile loop ([46]) is cyan, the N-terminal
extension of the apical domain ( [6]) is magenta, and helices H
and I are red.(A) Superposition of Cα coordinates of the apical
domain of three structures, showing the backbone of three
different peptides bound over the peptide-binding groove formed
by helix H and helix I. Structure of the helices displayed here
is taken from the structure of the SBP/apical domain
complex.(B–D) Molecular surfaces color coded by curvature
(green for convex, and gray for concave) of the binding groove
in SBP/apical domain, GroEL/GroES/(ADP)[7], and N-terminal
extension/apical domain, respectively. The orientation in these
three figures is the same as in (A). For clarity, only side
chains of residues located at the C-terminal arms of the β turn
of the SBP (starting from W7) and the GroES mobile loop
(starting from I25) are shown, as these segments form most of
the contacts with the binding site. The N-terminal arms of the
β turn of these two peptides are shown as a Cα trace. Residues
in the peptides that form extensive side chain interactions with
the binding site are labeled.(A) was produced using MOLSCRIPT
and RASTER 3D ([22 and 31]), and (B)–(D) were generated with
GRASP ( [32]).
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