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TitleMutation of Tyr137 of the universal Escherichia coli fimbrial adhesin FimH relaxes the tyrosine gate prior to mannose binding.
Journal, issue, pagesIUCrJ, Vol. 4, Page 7-23, Year 2017
Publish dateOct 6, 2013 (structure data deposition date)
AuthorsRabbani, S. / Krammer, E.M. / Roos, G. / Zalewski, A. / Preston, R. / Eid, S. / Zihlmann, P. / Prevost, M. / Lensink, M.F. / Thompson, A. ...Rabbani, S. / Krammer, E.M. / Roos, G. / Zalewski, A. / Preston, R. / Eid, S. / Zihlmann, P. / Prevost, M. / Lensink, M.F. / Thompson, A. / Ernst, B. / Bouckaert, J.
External linksIUCrJ / PubMed:28250938
MethodsX-ray diffraction
Resolution1.42 - 2.84 Å
Structure data

PDB-4ca4:
Crystal structure of FimH lectin domain with the Tyr48Ala mutation, in complex with heptyl alpha-D-mannopyrannoside
Method: X-RAY DIFFRACTION / Resolution: 2.84 Å

PDB-5fs5:
Breaking down the wall: mutation of the tyrosine gate of the universal Escherichia coli fimbrial adhesin FimH
Method: X-RAY DIFFRACTION / Resolution: 1.42 Å

PDB-5fwr:
Breaking down the wall: mutation of the tyrosine gate of the universal Escherichia coli fimbrial adhesin FimH
Method: X-RAY DIFFRACTION / Resolution: 2.13 Å

PDB-5fx3:
Breaking down the wall: mutation of the tyrosine gate of the universal Escherichia coli fimbrial adhesin FimH
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-KGM:
heptyl alpha-D-mannopyranoside / detergent*YM

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-3X8:
biphenyl-4-yl alpha-D-mannopyranoside

ChemComp-EDT:
{[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC ACID

Source
  • escherichia coli (E. coli)
KeywordsCELL ADHESION / BACTERIAL ADHESIN / TYPE 1 FIMBRIAE / URINARY TRACT INFECTION / VARIABLE IMMUNOGLOBULIN FOLD / HEPTYL MANNOSE / FIMH ANTAGONIST

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