Figure 1.
Figure 1. Stereo ribbon drawing of one subunit of the trimeric
TSP N
prepared with MOLMOL.[59] The domain formed by the large
right-handed -helix
is in dark grey. Thirteen complete turns wind around the helix
axis and form a long binding groove for the lipopolysaccharide
receptor of phage P22 present on the surface of its host
Salmonella. Bound octasaccharide, a product of the hydrolysis
catalysed by the endorhamnosidase, is indicated by thick lines.
The mutation sites addressed here are indicated as light
spheres. The N-terminus is located in the lower left.
N
prepared with MOLMOL.[59] The domain formed by the large
right-handed 
-helix
is in dark grey. Thirteen complete turns wind around the helix
axis and form a long binding groove for the lipopolysaccharide
receptor of phage P22 present on the surface of its host
Salmonella. Bound octasaccharide, a product of the hydrolysis
catalysed by the endorhamnosidase, is indicated by thick lines.
The mutation sites addressed here are indicated as light
spheres. The N-terminus is located in the lower left.