Structural highlights
Function
Q9A753_CAUVC
Publication Abstract from PubMed
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 beta helix with six windings and a triangular hydrophobic core. The BacA structure was determined to 1.0 A 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.
Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR.,Shi C, Fricke P, Lin L, Chevelkov V, Wegstroth M, Giller K, Becker S, Thanbichler M, Lange A Sci Adv. 2015 Dec 4;1(11):e1501087. doi: 10.1126/sciadv.1501087. eCollection 2015, Dec. PMID:26665178[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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 4;1(11):e1501087. doi: 10.1126/sciadv.1501087. eCollection 2015, Dec. PMID:26665178 doi:http://dx.doi.org/10.1126/sciadv.1501087
