Select & Highlight:
  "a-positions"
  "d-positions"

  Heptad units:
  1   2   3
  4   5   6
  7   8
  Select All
  Rotate:
  X 90°   X -90°
  Y 90°   Y -90°
  Distances:
  Length
   (in Å units).
  Width
   (in Å units).
  Reset
Highlight the residues that are the same or different in the Janus protein of Dalal, S., et al. (1997) "Protein alchemy: Changing b-sheet into a-helix"Nature Struct. Biol.7, 548. Consult their Fig. 1c for details.
  The positions in Janus that are identical in Rop are colored red.
  The positions in Janus that are identical in Protein G are colored light blue.
  The positions in Janus that are identical in Rop and Protein G are colored green.
    (All other residues retain their original colors.)
View a helical wheel diagram of Rop protein in a pop-up window. The diagram is a useful complement to the Chime image and vice versa.
Rop Protein DimerOverall Architecture of the Rop Protein Dimer.
The starting display of this four-helix bundle protein is wireframe with a backbone trace. The A subunit of the homodimer is colored white; the B subunit is colored cyan. The amino- and carboxyl-termini of each chain are labeled.
Viewing Suggestions:
1. The "Select & Highlight" buttons color the "a-position" sidechains green and the "d-position" sidechains pink. Together, these residues make up the hydrophobic core of the structure. (Each button also leaves the image with the corresponding sidechains selected; thus, alternative color or display choices can be chosen for each group from the Chime menu.)
2. The "Heptad units" buttons highlight consecutive seven-amino acid segments of chain B and label the a-postion and d-postion amino acids in each group. After highlighting a unit, choose Spacefill and CPK from the Chime menu to see how each pair of amino acids packs against the sidechains of chain A.
3. The rotate buttons act on the entire structure. Remove the distance monitors with a second click.
4. After highlighting the core residues, view the structure end-on; then slab through the length of the four-helix bundle to see the packing of the highlighted side chains. (Select Slab Mode in the Chime Options menu and hold the control key down while dragging the mouse vertically in the image.)
The dimer shown here is the "Biological functional unit" derived from the monomer coordinates (1rop.pdb).
Banner, D. W. et al. (1987) "Structure of the ColE1 rop protein at 1.7 Å resolution"J. Mol. Biol.196, 657.
The boxed area below contains a RasMol script that will produce the starting display on this page; it then highlights the a-position and d-postion residues sequentially. (Select and copy the text in the box for viewing in RasMol.)

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