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  Hybrid structure of the type 1 pilus of uropathogenic Escherichia coli.

Habenstein, B., Loquet, A., Hwan, S., Giller, K., Vasa, S. K., Becker, S., et al. (2015). Hybrid structure of the type 1 pilus of uropathogenic Escherichia coli. Angewandte Chemie International Edition, 54(40), 11691-11695. doi:10.1002/anie.201505065.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-8F43-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-2F68-0
Genre: Journal Article

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 Creators:
Habenstein, B.1, Author              
Loquet, A.1, Author              
Hwan, S.1, Author              
Giller, K.2, Author              
Vasa, S. K.1, Author              
Becker, S.2, Author              
Habeck, M.3, Author              
Lange, A.1, Author              
Affiliations:
1Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society, ou_persistent35              
2Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
3Research Group of Statistical Inverse-Problems in Biophysics, MPI for Biophysical Chemistry, Max Planck Society, ou_1113580              

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Free keywords: filamentous protein assemblies;iterative modeling;pilus structure;solid-state NMR spectroscopy;structure elucidation
 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.

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Language(s): eng - English
 Dates: 2015-08-122015-09-28
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201505065
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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 54 (40) Sequence Number: - Start / End Page: 11691 - 11695 Identifier: -