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Angew Chem Int Ed Engl. 2015 Sep 28;54(40):11691-5. doi: 10.1002/anie.201505065. Epub 2015 Aug 12.

Hybrid Structure of the Type 1 Pilus of Uropathogenic Escherichia coli.

Author information

1
Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen (Germany).
2
Université de Bordeaux/CBMN UMR5248, Institut Européen de Chimie et Biologie (IECB), 2 rue Robert Escarpit, 33600 Pessac (France).
3
Institut für Biologie, Humboldt-Universität zu Berlin, Invalidenstrasse 110, 10115 Berlin (Germany).
4
Department of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie (FMP), Robert-Rössle-Strasse 10, 13125 Berlin (Germany).
5
Felix Bernstein Institute for Mathematical Statistics in the Biosciences, University of Göttingen, Goldschmidtstrasse 7, 37077 Göttingen (Germany). mhabeck@gwdg.de.
6
Statistical Inverse Problems in Biophysics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen (Germany). mhabeck@gwdg.de.
7
Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen (Germany). alange@fmp-berlin.de.
8
Institut für Biologie, Humboldt-Universität zu Berlin, Invalidenstrasse 110, 10115 Berlin (Germany). alange@fmp-berlin.de.
9
Department of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie (FMP), Robert-Rössle-Strasse 10, 13125 Berlin (Germany). alange@fmp-berlin.de.

Abstract

Type 1 pili are filamentous protein assemblies on the surface of Gram-negative bacteria that mediate adhesion to host cells during the infection process. The molecular structure of type 1 pili remains elusive on the atomic scale owing to their insolubility and noncrystallinity. Herein we describe an approach for hybrid-structure determination that is based on data from solution-state NMR spectroscopy on the soluble subunit and solid-state NMR spectroscopy and STEM data on the assembled pilus. Our approach is based on iterative modeling driven by structural information extracted from different sources and provides a general tool to access pseudo atomic structures of protein assemblies with complex subunit folds. By using this methodology, we determined the local conformation of the FimA pilus subunit in the context of the assembled type 1 pilus, determined the exact helical pilus architecture, and elucidated the intermolecular interfaces contributing to pilus assembly and stability with atomic detail.

KEYWORDS:

filamentous protein assemblies; iterative modeling; pilus structure; solid-state NMR spectroscopy; structure elucidation

PMID:
26267365
DOI:
10.1002/anie.201505065
[Indexed for MEDLINE]

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