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

Loquet A, Habenstein B, Chevelkov V, Vasa SK, Giller K, Becker S, Lange A
J Am Chem Soc 135 19135-8 (2013)
Cited: 9 times
EuropePMC logo PMID: 24328247

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.

Articles - 2mex mentioned but not cited (1)

  1. Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy. Loquet A, Tolchard J, Berbon M, Martinez D, Habenstein B. J Vis Exp (2017)


Reviews citing this publication (3)

  1. Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy. Quinn CM, Polenova T. Q Rev Biophys 50 e1 (2017)
  2. Selective labeling and unlabeling strategies in protein solid-state NMR spectroscopy. Lacabanne D, Meier BH, Böckmann A. J Biomol NMR 71 141-150 (2018)
  3. Solid-state NMR spectroscopic trends for supramolecular assemblies and protein aggregates. Linser R. Solid State Nucl Magn Reson 87 45-53 (2017)

Articles citing this publication (5)

  1. High-resolution structure of the Shigella type-III secretion needle by solid-state NMR and cryo-electron microscopy. Demers JP, Habenstein B, Loquet A, Kumar Vasa S, Giller K, Becker S, Baker D, Lange A, Sgourakis NG. Nat Commun 5 4976 (2014)
  2. Structure determination of helical filaments by solid-state NMR spectroscopy. He L, Bardiaux B, Ahmed M, Spehr J, König R, Lünsdorf H, Rand U, Lührs T, Ritter C. Proc Natl Acad Sci U S A 113 E272-81 (2016)
  3. Reassessment of MxiH subunit orientation and fold within native Shigella T3SS needles using surface labelling and solid-state NMR. Verasdonck J, Shen DK, Treadgold A, Arthur C, Böckmann A, Meier BH, Blocker AJ. J Struct Biol 192 441-448 (2015)
  4. Strategies for solid-state NMR investigations of supramolecular assemblies with large subunit sizes. Fricke P, Chevelkov V, Shi C, Lange A. J Magn Reson 253 2-9 (2015)
  5. Specific 13C labeling of leucine, valine and isoleucine methyl groups for unambiguous detection of long-range restraints in protein solid-state NMR studies. Fasshuber HK, Demers JP, Chevelkov V, Giller K, Becker S, Lange A. J Magn Reson 252 10-19 (2015)


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