RMSD analysis of structures of the bacterial protein FimH identifies five conformations of its lectin domain-Reference-Cited by-同舟云学术

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RMSD analysis of structures of the bacterial protein FimH identifies five conformations of its lectin domain

Published:2019-11-05 Issue:4 Volume:88 Page:593-603
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Magala Pearl¹²,Klevit Rachel E.¹²,Thomas Wendy E.³,Sokurenko Evgeni V.⁴,Stenkamp Ronald E.¹²⁵^ORCID

Affiliation:

1. Department of BiochemistryUniversity of Washington Seattle WA

2. Biomolecular Structure CenterUniversity of Washington Seattle WA

3. Department of BioengineeringUniversity of Washington Seattle WA

4. Department of MicrobiologyUniversity of Washington Seattle WA

5. Department of Biological StructureUniversity of Washington Seattle WA

Funder

National Institute of Allergy and Infectious Diseases

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.25840

Reference43 articles.

1. Bacterial Adherence: Adhesin-Receptor Interactions Mediating the Attachment of Bacteria to Mucosal Surfaces

2. FimH adhesin of type 1 pili is assembled into a fibrillar tip structure in the Enterobacteriaceae.

3. Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin

4. Pili in Gram-negative and Gram-positive bacteria — structure, assembly and their role in disease

5. Crystal structure of the FimD usher bound to its cognate FimC–FimH substrate

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