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Figure 2.
Figure 2. Key Interactions at the Sse1p·ATP-Hsp70N
Interface
(A) Closeup view of the contacts between
subdomain IIb of Hsp70N and the 3HBD of Sse1p.
(B) Contact
interface in the vicinity of the Sse1p-bound ATP molecule.
(C) Region of close surface complementarity between Sse1p and
subdomain Ia of Hsp70N.
In (A)–(C), both protein
backbones are shown in ribbon representation with the exception
of regions involved in intermolecular contacts. These regions
and the corresponding side chains are depicted in stick
representation. Sse1p is enveloped in a transparent molecular
surface to highlight the close surface complementarity. The
color coding for molecular surfaces, backbone, and carbon atoms
is identical to that in Figure 1A. Sse1p-bound ATP is
represented in a ball-and-stick model with carbon atoms colored
in yellow. Nitrogen and oxygen atoms are indicated in blue and
red, respectively. Ordered water molecules bridging the binding
partners are shown as beige spheres. Hydrogen bonds are
represented as dashed lines. Key interacting residues are
indicated. In all panels, unrelated obstructing features in the
foreground were omitted for clarity.
(D) Alignment of
Hsp110, Hsp70, and DnaK amino acid sequences at the contact
region between the 3HBD of Sse1p and subdomain IIb of Hsp70N.
Contacting residues are indicated below the sequence with the
interacting domain indicated by the color scheme used in Figure
1A. Notable differences in the consensus sequences for Hsp110s
and canonical Hsp70s are boxed. An unabridged version of the
alignment is shown in Figure S5.
(E) Sequence alignment of
residues involved in the contact close to the nucleotide-binding
pocket of Sse1p.
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