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Journal Article

Atomic structure and handedness of the building block of a biological assembly.

MPS-Authors
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Loquet,  A.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

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Habenstein,  B.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

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Chevelkov,  V.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

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Vasa,  S. K.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Giller,  K.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Lange,  A.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

External Ressource
Fulltext (public)

1921620.pdf
(Publisher version), 2MB

Supplementary Material (public)

1921620_Suppl_1.pdf
(Supplementary material), 2MB

Citation

Loquet, A., Habenstein, B., Chevelkov, V., Vasa, S. K., Giller, K., Becker, S., et al. (2013). Atomic structure and handedness of the building block of a biological assembly. Journal of the American Chemical Society, 135(51), 19135-19138. doi:10.1021/ja411362q.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0015-36A0-1
Abstract
Noncovalent supramolecular assemblies possess in general several unique subunit subunit interfaces.The basic building block of such an assembly consists of several subunits and contains all unique interfaces. Atomic-resolution structures of monomeric subunits are typically accessed by crystallography or solution NMR and fitted into electron microscopy density maps. However, the structure of the intact building block in the assembled state remains unknown with this hybrid approach. Here, we present the solid-state NMR atomic structure of the building block of the type III secretion system needle. The building block structure consists of a homotetrameric subunit complex with three unique supramolecular interfaces. Side-chain positions at the interfaces were solved at atomic detail. The high-resolution structure reveals unambiguously the helical handedness of the assembly, determined to be right-handed for the type III secretion system needle.Additionally, the axial rise per subunit could be extracted from the tetramer structure and independently validated by mass-per-length measurements.