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

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

The most prevalent diseases manifested by Escherichia coli are acute and recurrent bladder infections and chronic inflammatory bowel diseases such as Crohn's disease. E. coli clinical isolates express the FimH adhesin, which consists of a mannose-specific lectin domain connected via a pilin dom...

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Bibliographic Details
Main Authors: Said Rabbani, Eva-Maria Krammer, Goedele Roos, Adam Zalewski, Roland Preston, Sameh Eid, Pascal Zihlmann, Martine Prévost, Marc F. Lensink, Andrew Thompson, Beat Ernst, Julie Bouckaert
Format: Article
Language:English
Published: International Union of Crystallography 2017-01-01
Series:IUCrJ
Subjects:
Escherichia coli infection
FimH adhesin
tyrosine gate
mutations
crystals
thermodynamics
peptide torsions
heptyl mannose
biphenyl mannose
molecular dynamics
protein structure
molecular recognition
X-ray crystallography
Online Access:http://scripts.iucr.org/cgi-bin/paper?S2052252516016675

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http://scripts.iucr.org/cgi-bin/paper?S2052252516016675

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