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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Vasa, Suresh Lin, Lin Thanbichler, Martin Riedel, Dietmar Lange, Adam Shi, Chaowei Kühn, Juliane Habenstein, Birgit |
| Description | Author Affiliation: Vasa S ( Department of NMR-Based Structural Biology and.); Lin L ( Prokaryotic Cell Biology Group, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany); Shi C ( Department of NMR-Based Structural Biology and Department of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany); Habenstein B ( Department of NMR-Based Structural Biology and.); Riedel D ( Electron Microscopy Group, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany); Kühn J ( Prokaryotic Cell Biology Group, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany); Thanbichler M ( Prokaryotic Cell Biology Group, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany); Lange A ( Department of NMR-Based Structural Biology and Department of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany); |
| Abstract | Bactofilins are a widespread class of bacterial filament-forming proteins, which serve as cytoskeletal scaffolds in various cellular pathways. They are characterized by a conserved architecture, featuring a central conserved domain (DUF583) that is flanked by variable terminal regions. Here, we present a detailed investigation of bactofilin filaments from Caulobacter crescentus by high-resolution solid-state NMR spectroscopy. De novo sequential resonance assignments were obtained for residues Ala39 to Phe137, spanning the conserved DUF583 domain. Analysis of the secondary chemical shifts shows that this core region adopts predominantly ß-sheet secondary structure. Mutational studies of conserved hydrophobic residues located in the identified ß-strand segments suggest that bactofilin folding and polymerization is mediated by an extensive and redundant network of hydrophobic interactions, consistent with the high intrinsic stability of bactofilin polymers. Transmission electron microscopy revealed a propensity of bactofilin to form filament bundles as well as sheet-like, 2D crystalline assemblies, which may represent the supramolecular arrangement of bactofilin in the native context. Based on the diffraction pattern of these 2D crystalline assemblies, scanning transmission electron microscopy measurements of the mass per length of BacA filaments, and the distribution of ß-strand segments identified by solid-state NMR, we propose that the DUF583 domain adopts a ß-helical architecture, in which 18 ß-strand segments are arranged in six consecutive windings of a ß-helix. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 2 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Bacterial Proteins Chemistry Caulobacter Crescentus Cytoskeleton Amino Acid Sequence Genetics Ultrastructure Conserved Sequence Electron Microscope Tomography Hydrophobic And Hydrophilic Interactions Microscopy, Electron, Transmission Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Multimerization Protein Structure, Secondary Structural Homology, Protein Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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