title: Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR.
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.
authors.affiliation: Department of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany.
authors.forename: Chaowei
authors.initials: C
authors.lastname: Shi
authors.affiliation: Department of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany.
authors.forename: Pascal
authors.initials: P
authors.lastname: Fricke
authors.affiliation: Prokaryotic Cell Biology Group, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany. ; Faculty of Biology, Philipps-Universität, 35043 Marburg, Germany.
authors.forename: Lin
authors.initials: L
authors.lastname: Lin
authors.affiliation: Department of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany.
authors.forename: Veniamin
authors.initials: V
authors.lastname: Chevelkov
authors.affiliation: Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
authors.forename: Melanie
authors.identifier: 0000-0002-3249-3917
authors.initials: M
authors.lastname: Wegstroth
authors.affiliation: Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
authors.forename: Karin
authors.identifier: 0000-0002-4149-7899
authors.initials: K
authors.lastname: Giller
authors.affiliation: Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.affiliation: 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.
authors.forename: Martin
authors.initials: M
authors.lastname: Thanbichler
authors.affiliation: Department of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany. ; Institut für Biologie, Humboldt-Universität zu Berlin, 10115 Berlin, Germany.
authors.forename: Adam
authors.initials: A
authors.lastname: Lange
keywords: Bactofilins; Cytoskeletal proteins; Protein Structure; Solid-state NMR