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  Atomic model of the type III secretion system needle.

Loquet, A., Sqourakis, N., Gupta, R., Giller, K., Riedel, D., Goosmann, C., et al. (2012). Atomic model of the type III secretion system needle. Nature, 486(7402), 276-279. doi:10.1038/nature11079.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000F-9E70-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-84E8-2
Genre: Journal Article

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 Creators:
Loquet, A.1, Author              
Sqourakis, N., Author
Gupta, R., Author
Giller, K.2, Author              
Riedel, D.3, Author              
Goosmann, C., Author
Griesinger, C.2, Author              
Kolbe, M., Author
Baker, D., Author
Becker, S.2, 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              
3Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              

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 Abstract: Pathogenic bacteria using a type III secretion system (T3SS)1, 2 to manipulate host cells cause many different infections including Shigella dysentery, typhoid fever, enterohaemorrhagic colitis and bubonic plague. An essential part of the T3SS is a hollow needle-like protein filament through which effector proteins are injected into eukaryotic host cells3, 4, 5, 6. Currently, the three-dimensional structure of the needle is unknown because it is not amenable to X-ray crystallography and solution NMR, as a result of its inherent non-crystallinity and insolubility. Cryo-electron microscopy combined with crystal or solution NMR subunit structures has recently provided a powerful hybrid approach for studying supramolecular assemblies7, 8, 9, 10, 11, 12, resulting in low-resolution and medium-resolution models13, 14, 15, 16, 17. However, such approaches cannot deliver atomic details, especially of the crucial subunit–subunit interfaces, because of the limited cryo-electron microscopic resolution obtained in these studies. Here we report an alternative approach combining recombinant wild-type needle production, solid-state NMR, electron microscopy and Rosetta modelling to reveal the supramolecular interfaces and ultimately the complete atomic structure of the Salmonella typhimurium T3SS needle. We show that the 80-residue subunits form a right-handed helical assembly with roughly 11 subunits per two turns, similar to that of the flagellar filament of S. typhimurium. In contrast to established models of the needle in which the amino terminus of the protein subunit was assumed to be α-helical and positioned inside the needle, our model reveals an extended amino-terminal domain that is positioned on the surface of the needle, while the highly conserved carboxy terminus points towards the lumen.

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Language(s): eng - English
 Dates: 2012-05-202012-06-14
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nature11079
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Title: Nature
Source Genre: Journal
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Pages: - Volume / Issue: 486 (7402) Sequence Number: - Start / End Page: 276 - 279 Identifier: -