|
Figure 1.
Figure 1. Crystal Structure of the Sse1p·ATP-Hsp70N
Complex
(A) Frontal view of the complex. Sse1p is shown in
ribbon representation with the NBD colored in dark blue, the
linker segment in yellow (in the background), and the β
sandwich and 3HBD in brown and green, respectively. The NBD of
human Hsp70, Hsp70N, is shown in surface representation in dark
red. The subdomain structure of Hsp70N is indicated.
(B)
Bottom view of the complex in surface representation using the
same coloring scheme as in (A).
(C) Cut-away views onto the
Hsp70N-Sse1p interface. The position of the interaction partner
is indicated by its outline. Interacting atoms are colored in
orange. Water molecules connecting the binding partners via
hydrogen bonds are indicated as beige spheres. ATP is shown in
ball-and-stick representation. The subdomain structures of the
NBDs are indicated.
(D) Surface conservation of the Sse1p
interface. The color gradient from red to cyan indicates
decreasing conservation. The corresponding representation for
the Hsp70N binding face can be found in Figure S2.
(E)
Superposition of the Hsp70N·ADP complex (light blue) with
Hsp70N from the Sse1p·ATP-Hsp70N structure (red). The
position of Sse1p is indicated by an outline. The orientation of
the structure is the same as in (C) and (D). Subdomain IIb of
the Hsp70N·ADP complex would clash with subdomain IIb in
Sse1p.
|
