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 domain t...

Täydet tiedot

Bibliografiset tiedot

Päätekijät:	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
Aineistotyyppi:	Artigo
Kieli:	Inglês
Julkaistu:	International Union of Crystallography 2017-01-01
Sarja:	IUCrJ
Aiheet:	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
Linkit:	http://scripts.iucr.org/cgi-bin/paper?S2052252516016675
Tagit:	Lisää tagi Ei tageja, Lisää ensimmäinen tagi!