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Shi C, Fricke P, Lin L, et al. Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR. Sci Adv. 2015;1(11):e1501087doi: 10.1126/sciadv.1501087.
Shi, C., Fricke, P., Lin, L., Chevelkov, V., Wegstroth, M., Giller, K., Becker, S., Thanbichler, M., & Lange, A. (2015). Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR. Science advances, 1(11), e1501087. https://doi.org/10.1126/sciadv.1501087
Shi, Chaowei, et al. "Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR." Science advances vol. 1,11 (2015): e1501087. doi: https://doi.org/10.1126/sciadv.1501087
Shi C, Fricke P, Lin L, Chevelkov V, Wegstroth M, Giller K, Becker S, Thanbichler M, Lange A. Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR. Sci Adv. 2015 Dec 04;1(11):e1501087. doi: 10.1126/sciadv.1501087. eCollection 2015 Dec. PMID: 26665178; PMCID: PMC4672760.
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Sci Adv. 2015 Dec 04;1(11):e1501087. doi: 10.1126/sciadv.1501087. eCollection 2015 Dec.

Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR.

Science advances

Chaowei Shi, Pascal Fricke, Lin Lin, Veniamin Chevelkov, Melanie Wegstroth, Karin Giller, Stefan Becker, Martin Thanbichler, Adam Lange

Affiliations

  1. Department of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany.
  2. Prokaryotic Cell Biology Group, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany. ; Faculty of Biology, Philipps-Universität, 35043 Marburg, Germany.
  3. Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
  4. Prokaryotic Cell Biology Group, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany. ; Faculty of Biology, Philipps-Universität, 35043 Marburg, Germany. ; LOEWE Center for Synthetic Microbiology, Philipps-Universität, 35043 Marburg, Germany.
  5. Department of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany. ; Institut für Biologie, Humboldt-Universität zu Berlin, 10115 Berlin, Germany.

PMID: 26665178 PMCID: PMC4672760 DOI: 10.1126/sciadv.1501087

Abstract

Bactofilins are a recently discovered class of cytoskeletal proteins of which no atomic-resolution structure has been reported thus far. The bacterial cytoskeleton plays an essential role in a wide range of processes, including morphogenesis, cell division, and motility. Among the cytoskeletal proteins, the bactofilins are bacteria-specific and do not have a eukaryotic counterpart. The bactofilin BacA of the species Caulobacter crescentus is not amenable to study by x-ray crystallography or solution nuclear magnetic resonance (NMR) because of its inherent noncrystallinity and insolubility. We present the atomic structure of BacA calculated from solid-state NMR-derived distance restraints. We show that the core domain of BacA forms a right-handed β helix with six windings and a triangular hydrophobic core. The BacA structure was determined to 1.0 Å precision (heavy-atom root mean square deviation) on the basis of unambiguous restraints derived from four-dimensional (4D) HN-HN and 2D C-C NMR spectra.

Keywords: Bactofilins; Cytoskeletal proteins; Protein Structure; Solid-state NMR

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