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![[Figure 2]](jb5037fig2mag.jpg)
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Figure 2
Movement of the B repeat relative to the internalin domain. Colouring is as in Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif) . Chains A, B and C of InlB392_wt are shown in dark blue, blue and cyan, respectively. Crystal forms I and II of InlB392_T332E are shown in green and dark green, respectively. The Cα atoms of the C-terminal residues 391 are shown as spheres. Dashed purple lines indicate the distances between C-terminal residues. (a) Chains A (dark blue) and C (cyan) of InlB392_wt were aligned on the LRR region. (b) The view is rotated relative to (a) by 90° around a vertical axis. Crystal forms I (green) and II (dark green) of InlB392_T332E were aligned on the LRR region. (c) Overlay of all InlB392 structures aligned on the LRR region and shown from the top of the B repeat. (d) Residue Glu321 appears to be an integral part of the B repeat (top) rather than the internalin domain (bottom). Glu321 forms hydrogen bonds from its side chain to the hydroxyl group of Tyr323 and from its backbone carbonyl to the backbone N atom of Ala340. The only interaction with the internalin domain is a CH–π interaction with Phe290. |
![[Figure 2]](jb5037fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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