Figure 2.
Figure 2 (a) Structure of a typical LRR coil of internalin C,
comprising 22 residues. The LRR shown is coil four of six
present in InlC and corresponds to residues 141-162. The
hydrophobic core of the LRR domain is typically formed by
leucine residues at positions 2, 5, 7, 12, 15, 18 and 21. There
is an asparagine at position 10 in five out of the six turns;
the first turn is a variant and the first -strand
of the Ig-like domain provides an equivalent glutamine. (b)
Structure of the unique 21-residue coil three of InlC (residues
120-140). The 3[10]-helix of the other coils (see a) is missing,
replaced by a 1-4
turn (residues 15-18) and a proline at position 19.
The above figure is reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2006,
62,
1287-1293)
copyright 2006.
-strand
of the Ig-like domain provides an equivalent glutamine. (b)
Structure of the unique 21-residue coil three of InlC (residues
120-140). The 3[10]-helix of the other coils (see a) is missing,
replaced by a