1. Structure of the InlB Leucine-Rich Repeats, a Domain that Triggers Host Cell Invasion by the Bacterial Pathogen L. monocytogenes 
Michael Marino, Laurence Braun, Pascale Cossart, Partho Ghosh 
Molecular Cell 
Volume 4, Issue 6, Pages (December 1999)
DOI: /S (00)

2. Figure 1
InlB LRR Domain
α and 310 helices are in cyan, β strands are in red, and loops are in green. The domain consists of the N-terminal cap region (residues 36–76) and the LRR region (residues 77–242). Calciums are depicted as blue spheres. This and remaining figures were generated with MOLSCRIPT (Kraulis 1991) and Raster3D (Merrit and Bacon 1997).
Molecular Cell 1999 4, DOI: ( /S (00) )

3. Figure 2 Calcium-Binding N-Terminal Cap
(A) Structure of the N-terminal cap (residues 36–76). Calcium ions are depicted as blue spheres, and side chains that directly coordinate the calciums are shown, with carbons in orange and oxygens in red.
(B) Sequence alignment of cap regions of nine internalin family members. Secondary structure elements are depicted above the InlB sequence, and blue spheres denote InlB side chains that directly or indirectly contact calcium 1 or 2. Conserved residues that play a structural role in InlB are shaded. The last line shows the cap region consensus sequence, which contains the most commonly occurring residue in the internalin family.
Molecular Cell 1999 4, DOI: ( /S (00) )

4. Figure 3
Calcium Sites
(A) Calcium site 1. The calcium is depicted as a blue sphere, and waters are depicted as red spheres. Calcium–oxygen coordination is shown with solid black lines, and hydrogen bonds are shown with dotted black lines. Gray, main chain carbons; orange, side chain carbons; blue, nitrogens; red, oxygens.
(B) Calcium site 2. The depiction is the same as in (A).
(C) Quantitation of calcium affinity by integration of electron densities for calciums 1 and 2.
(D) Magnesium bound to site 1. The view and depiction scheme are the same as in (A).
Molecular Cell 1999 4, DOI: ( /S (00) )

5. Figure 4
Water Spines
The convex face of the InlB LRR region faces the viewer. Waters are depicted as red spheres. The hydrogen bonding scheme is shown below, with atoms numbered by their position within the LRR. The numbering convention of the InlB LRR follows that of the RI LRR (Kobe and Deisenhofer 1995), with the β strand occupying positions 4–6. The spines are named according to the first LRR position that forms a hydrogen bond with the water. Between the third and fourth repeats in Spine 15, two waters are accommodated due to a local increase in the curvature of the molecule. Gln-165 occupies the position of a water in Spine 1 between the same two repeats.
Molecular Cell 1999 4, DOI: ( /S (00) )

6. Figure 5 Leucine-Rich Repeats
(A) Structure of a single 22-residue InlB LRR. Backbone carbons are gray; side chain carbons of conserved or restricted residues are orange; nitrogens and oxygens are blue and red, respectively. Hydrogen bonds are shown as black dotted lines. The location of the β strand and 310-helix are shown for reference. Repeat positions 7 to 10 form a distorted type II (βPγ) turn, and repeat positions 21 to 2 (of the following repeat) form a type I (αα) turn.
(B) Alignment of the seven and one-half LRRs of InlB (residues 77–242). The consensus repeat sequence is shown below and contains the most commonly occurring residue; the “s” at position 17 denotes a small residue.
Molecular Cell 1999 4, DOI: ( /S (00) )

7. Figure 6 Potential Protein–Protein Interaction Sites
(A) (Left) InlB LRR domain shown as a Cα trace with the concave side facing the viewer. Side chains that form a hydrophobic cluster (Ile-82, Phe-104, Trp-124, Phe-126, Tyr-170, Tyr-214, Val-234, and Phe-238) are shown with carbons in green. Side chains that form a negative cluster (Asp-128, Glu-129, Glu-150, Glu-194, Asp-160, and Glu-236) are shown with carbons in yellow. Calciums are shown as yellow spheres.
(Middle) Molecular surface of InlB LRR domain, colored green for hydrophobic residues and blue for calcium.
(Right) Electrostatic potential mapped on the molecular surface of the InlB LRR domain with calcium bound. Red is negative (−10 kT), and blue is positive (+10 kT). Calcium is indicated by numbering.
(B) Same depiction as in (A) with the molecule rotated 90° counterclockwise (along the long axis of the molecule).
Molecular Cell 1999 4, DOI: ( /S (00) )