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2n3d
From Proteopedia
(Difference between revisions)
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n3d OCA], [http://pdbe.org/2n3d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n3d RCSB], [http://www.ebi.ac.uk/pdbsum/2n3d PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n3d OCA], [http://pdbe.org/2n3d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n3d RCSB], [http://www.ebi.ac.uk/pdbsum/2n3d PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:26665178</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2n3d" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 04:50, 7 January 2016
Atomic structure of the cytoskeletal bactofilin BacA revealed by solid-state NMR
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Categories: Becker, S | Chevelkov, V | Fricke, P | Giller, K | Lange, A | Lin, L | Shi, C | Thanbichler, M | Wegstroth, M | Baca | Bactofilin | Beta helix | Cell shape | Cytoskeleton | Structural protein
