 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](be5063fig2mag.jpg)
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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 β-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 310-helix of the other coils (see a) is missing, replaced by a β1–4 turn (residues 15–18) and a proline at position 19. |
![[Figure 2]](be5063fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
