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Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR
Chaowei Shi
Pascal Fricke
Lin Lin
Veniamin Chevelkov
Melanie Wegstroth
Karin Giller
Stefan Becker
Martin Thanbichler
Adam Lange
Science Advances, 1(11), pp e1501087, 2015-12
Summary
<jats:p>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 <jats:italic>Caulobacter crescentus</jats:italic> 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.</jats:p>
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