Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR.
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.
['Shi|Chaowei|C|', 'Fricke|Pascal|P|', 'Lin|Lin|L|', 'Chevelkov|Veniamin|V|', 'Wegstroth|Melanie|M|0000-0002-3249-3917', 'Giller|Karin|K|0000-0002-4149-7899', 'Becker|Stefan|S|', 'Thanbichler|Martin|M|', 'Lange|Adam|A|']
Bactofilins Solid-state NMR Cytoskeletal proteins Protein Structure