Close up de citoesqueleto bacteriano em nível atômico-molecular

terça-feira, dezembro 08, 2015

Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR

Chaowei Shi1,†, Pascal Fricke1,†, Lin Lin2,3,‡, Veniamin Chevelkov1, Melanie Wegstroth4, Karin Giller4, Stefan Becker4, Martin Thanbichler2,3,5 and Adam Lange1,6,§

- Author Affiliations

1Department of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany.
2Prokaryotic Cell Biology Group, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany.
3Faculty of Biology, Philipps-Universität, 35043 Marburg, Germany.
4Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
5LOEWE Center for Synthetic Microbiology, Philipps-Universität, 35043 Marburg, Germany.
6Institut für Biologie, Humboldt-Universität zu Berlin, 10115 Berlin, Germany.

↵§Corresponding author. E-mail:

↵* Presented in part at the Gordon Research Conference “Computational Aspects—Biomolecular NMR” (Il Ciocco, 7 to 12 June 2015).

↵† These authors contributed equally to this work.

↵‡ Present address: Focal Area Infection Biology, Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland.

Science Advances  04 Dec 2015:
Vol. 1, no. 11, e1501087
DOI: 10.1126/sciadv.1501087


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.
KeywordsCytoskeletal proteinsBactofilinsProtein StructureSolid-state NMR

Copyright © 2015, The Authors

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