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  High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy.

Demers, J. P., Habenstein, B., Loquet, A., Vasa, S. K., Giller, K., Becker, S., et al. (2014). High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy. Nature Communications, 5: 4976. doi:10.1038/ncomms5976.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-291B-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-48CB-A
Genre: Journal Article

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 Creators:
Demers, J. P.1, Author              
Habenstein, B.1, Author              
Loquet, A.1, Author              
Vasa, S. K.1, Author              
Giller, K.2, Author              
Becker, S.2, Author              
Baker, D., Author
Lange, A.1, Author              
Sgourakis, N. G., 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              

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 Abstract: We introduce a general hybrid approach for determining the structures of supramolecular assemblies. Cryo-electron microscopy (cryo-EM) data define the overall envelope of the assembly and rigid-body orientation of the subunits while solid-state nuclear magnetic resonance (ssNMR) chemical shifts and distance constraints define the local secondary structure, protein fold and inter-subunit interactions. Finally, Rosetta structure calculations provide a general framework to integrate the different sources of structural information. Combining a 7.7-EM density map and 996 ssNMR distance constraints, the structure of the type-III secretion system needle of Shigella flexneri is determined to a precision of 0.4 angstrom. The calculated structures are cross-validated using an independent data set of 691 ssNMR constraints and scanning transmission electron microscopy measurements. The hybrid model resolves the conformation of the non-conserved N terminus, which occupies a protrusion in the cryo-EM density, and reveals conserved pore residues forming a continuous pattern of electrostatic interactions, thereby suggesting a mechanism for effector protein translocation.

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Language(s): eng - English
 Dates: 2014-09-29
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/ncomms5976
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Title: Nature Communications
Source Genre: Journal
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Pages: 12 Volume / Issue: 5 Sequence Number: 4976 Start / End Page: - Identifier: -