Mutation of Tyr137 of the universal Escherichia coli fimbrial adhesin FimH relaxes the tyrosine gate prior to mannose binding

Rabbani, S.; Krammer, E.-M.; Roos, G.; Zalewski, A.; Preston, R.; Eid, S.; Zihlmann, P.; Prévost, M.; Lensink, M.F.; Thompson, A.; Ernst, B.; Bouckaert, J.

doi:10.1107/S2052252516016675

Figure 9
The different processes identified to play a role in the change in FimH affinity for binding (a) HM and (b) BF upon mutation of one of the tyrosine-gate residues. Both the results from the ITC measurements (Table 3

) and from the molecular simulation (MD and QM; see §§3.5–3.8

) are summarized.

IUCrJ

Volume 4| Part 1| January 2017| Pages 7-23

ISSN: 2052-2525

https://doi.org/10.1107/S2052252516016675

BIOLOGY | MEDICINE

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