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Journal ArticleDOI

X-ray Structure of the FimC-FimH Chaperone-Adhesin Complex from Uropathogenic Escherichia coli

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TLDR
The x-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5 angstrom resolution reveals the basis for carbohydrate recognition and for pilus assembly.
Abstract
Type 1 pili—adhesive fibers expressed in most members of the Enterobacteriaceae family—mediate binding to mannose receptors on host cells through the FimH adhesin. Pilus biogenesis proceeds by way of the chaperone/usher pathway. The x-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5 angstrom resolution reveals the basis for carbohydrate recognition and for pilus assembly. The carboxyl-terminal pilin domain of FimH has an immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand complementation mechanism in which the chaperone donates a strand to complete the pilin domain explains the basis for both chaperone function and pilus biogenesis.

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Citations
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Journal ArticleDOI

Secretion systems in Gram-negative bacteria: structural and mechanistic insights

TL;DR: The structural and mechanistic relationships between these single- and double-membrane-embedded systems are explored, and how this knowledge can be exploited for the development of new antimicrobial strategies are discussed.
Journal ArticleDOI

Type 1 pilus‐mediated bacterial invasion of bladder epithelial cells

TL;DR: The results demonstrate that UPEC strains are not strictly extracellular pathogens and that the type 1 pilus adhesin FimH can directly trigger host cell signaling cascades that lead to bacterial internalization.
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From carbohydrate leads to glycomimetic drugs

TL;DR: Examples of approved carbohydrate-derived drugs are examined, the potential of carbohydrate-binding proteins as new drug targets are discussed (focusing on the lectin families) and ways to overcome the challenges of developing this unique class of novel therapeutics are considered.
Journal ArticleDOI

Bacterial adhesion to target cells enhanced by shear force.

TL;DR: The ability of FimH to function as a force sensor provides a molecular mechanism for discrimination between surface-exposed and soluble receptor molecules and extension of the interdomain linker chain under mechanical force is indicated.
Journal ArticleDOI

Carbohydrates as future anti-adhesion drugs for infectious diseases.

TL;DR: There is little doubt that inhibitors of microbial lectins will in the near future join the arsenal of drugs for therapy of infectious diseases, and polyvalent saccharides are also powerful inhibitors of bacterial adhesion in vitro.
References
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Journal ArticleDOI

Clustal w: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

TL;DR: The sensitivity of the commonly used progressive multiple sequence alignment method has been greatly improved and modifications are incorporated into a new program, CLUSTAL W, which is freely available.
Book ChapterDOI

Processing of X-ray diffraction data collected in oscillation mode

TL;DR: The methods presented in the chapter have been applied to solve a large variety of problems, from inorganic molecules with 5 A unit cell to rotavirus of 700 A diameters crystallized in 700 × 1000 × 1400 A cell.
Journal ArticleDOI

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

TL;DR: The MOLSCRIPT program as discussed by the authors produces plots of protein structures using several different kinds of representations, including simple wire models, ball-and-stick models, CPK models and text labels.
Journal ArticleDOI

Improved methods for building protein models in electron density maps and the location of errors in these models.

TL;DR: In this paper, the authors describe strategies and tools that help to alleviate this problem and simplify the model-building process, quantify the goodness of fit of the model on a per-residue basis and locate possible errors in peptide and side-chain conformations.
Journal ArticleDOI

Protein structure comparison by alignment of distance matrices

TL;DR: A novel algorithm (DALI) for optimal pairwise alignment of protein structures that identifies structural resemblances and common structural cores accurately and sensitively, even in the presence of geometrical distortions is developed.
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