|
Figure 1.
Figure 1. Crystal Structure of the HK853[CP]-RR468 Complex
and Expanded Views of the Contacts within the Complex
(A
and B) Ribbon diagrams of the complex viewed from the cell
membrane along the twofold axis (indicated with a black ellipse)
(A) or perpendicularly to this axis (B), with the cell membrane
and the cell interior at the top and bottom, respectively. The
α helices of each HK protomer are colored blue (HK853[CP]) and
cyan (HK853[CP]^*), and the two RR468 molecules are shown in
gold (RR468) and light yellow (RR468^*), although β strands are
colored red in all cases. In (B), the RR468 molecule at the back
has been omitted for clarity. The side chains of the
phosphoacceptor H260 and D53 residues and the bound sulfate and
ADPβN molecules are illustrated in stick representation. In one
protomer of each HK853[CP] and RR468, secondary structure
elements and relevant loops have been labeled.
(C)
Six-helix bundle formed by the DHp domains of the two HK853[CP]
subunits (blue and cyan, and abbreviated HK) and by the α1
helices of both RR468 molecules (red and magenta, and
abbreviated RR). The orientation is similar to that in (B). Loop
β5-α5 is also shown for the RR molecule in the front.
(D)
Interactions between the β3-α3 loop of RR468 and the ATP lid
and β4-α4 loop of the CA domain of HK853, to illustrate the
interposition of the ATP lid between the secluded nucleotide and
His260 of the same subunit.
(E) Interactions of the RR468
β4-α4 loop (green) with the DHp-CA interdomain linker (cyan).
Side chains of interacting residues are shown with broken lines
indicating polar bonds.
|
