A recurring packing contact in crystals of InlB pinpoints functional binding sites in the internalin domain and the B repeat

Geerds, C.; Bleymüller, W.M.; Meyer, T.; Widmann, C.; Niemann, H.H.

doi:10.1107/S2059798322000432

Figure 5
Comparison of InlB₃₉₂ structures with the structure of full-length InlB (PDB entry 1m9s). Two symmetry-related copies of full-length InlB are shown in grey and pink, with the internalin domains at the bottom and the three GW domains at the top. C^α atoms of the last residue of the grey internalin domain (residue 319) and of residue 393 at the beginning of the GW domains are shown as spheres. Because there was no interpretable density for the B repeat, it was unclear which GW domains should be grouped with the grey internalin domain. Ghosh and coworkers deposited the asymmetric unit containing a combination of the internalin domain and GW domains with the shorter distance. The other choice of asymmetric unit (grey internalin domain and pink GW domains) would result in only a slightly longer distance. All InlB₃₉₂ structures were structurally aligned on the grey internalin domain. Colouring is as in Fig. 1

. 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. C^α atoms of the C-terminal residues (391 or 392) are shown as red spheres. Crystal form II of InlB₃₉₂_T332E has the shortest distance of 9.0 Å between its C-terminal residue 392 and residue 393 of the pink GW domains. All distances are shown as purple dashed lines.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 78| Part 3| March 2022| Pages 310-320

https://doi.org/10.1107/S2059798322000432

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