Figure 1 - full size

 

Figure 1.
Figure 1. a, Ribbon representation of the EcoRV dimer showing the dimerization domain at bottom (orange), the DNA-binding/catalytic domains in yellow and the four flexible linkers I−IV in each subunit^13. The major-groove binding R-loops (red, residues 182−188 of each subunit) present all of the primary determinants for direct readout of base-pair functional groups in the GATATC target. The scissile phosphorus atoms are shown by the pink spheres. The Gln-rich Q-loops that bind in the minor groove are shown in blue. b, View of the bent DNA conformation as seen in the complex of EcoRV with specific DNA^13. The center TA step and the R-loops are drawn in purple and blue, respectively. Van der Waals contacts of the Thr 186 side-chain methyl groups (red) with functional groups in the major groove are shown. c, Hydrogen-bonding (dotted lines) and van der Waals/electrostatic contacts (hatched lines) at the center TA step in the wild-type EcoRV−DNA complex. Distances in Å between nonhydrogen atoms are from the ternary complex structure with Ca^2+ (ref. 15). The contacts between Thr 186 and the thymine O4/adenine N6 groups may contribute binding energy but are considered to be nonspecific. The Watson−Crick hydrogen bonds are designated WC. The distance between the Thr 186 and Thr 186' methyl groups from the two separate subunits is 4.2 Å.

The above figure is reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (1999, 6, 269-277) copyright 1999.