2N3D

Atomic structure of the cytoskeletal bactofilin BacA revealed by solid-state NMR

Summary for 2N3D

• Entry DOI: 10.2210/pdb2n3d/pdb
• NMR Information: BMRB: 25642
• Descriptor: Bactofilin A (1 entity in total)
• Functional Keywords: baca, bactofilin, cell shape, cytoskeleton, beta helix, structural protein
• Biological source: Caulobacter crescentus
• Total number of polymer chains: 1
• Total formula weight: 19369.78

Authors

Shi, C.,Fricke, P.,Lin, L.,Chevelkov, V.,Wegstroth, M.,Giller, K.,Becker, S.,Thanbichler, M.,Lange, A. (deposition date: 2015-05-29, release date: 2015-12-16, Last modification date: 2024-05-15)

Primary citation

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, 1:e1501087-e1501087, 2015

PubMed 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.

PubMed: 26665178
DOI: 10.1126/sciadv.1501087

Experimental method

SOLID-STATE NMR