Download MendeleyCrystal structure of a naturally occurring parallel right-handed coiled coil tetramer.
Stetefeld, J., Jenny, M., Schulthess, T., Landwehr, R., Engel, J., Kammerer, R.A.(2000) Nat Struct Biol 7: 772-776
- PubMed: 10966648
- DOI: https://doi.org/10.1038/79006
- Primary Citation of Related Structures:
1FE6 - PubMed Abstract:
The crystal structure of a polypeptide chain fragment from the surface layer protein tetrabrachion from Staphylothermus marinus has been determined at 1.8 A resolution. As proposed on the basis of the presence of 11-residue repeats, the polypeptide chain fragment forms a parallel right-handed coiled coil structure. Complementary hydrophobic interactions and complex networks of surface salt bridges result in an extremely thermostable tetrameric structure with remarkable properties. In marked contrast to left-handed coiled coil tetramers, the right-handed coiled coil reveals large hydrophobic cavities that are filled with water molecules. As a consequence, the packing of the hydrophobic core differs markedly from that of a right-handed parallel coiled coil tetramer that was designed on the basis of left-handed coiled coil structures.
Organizational Affiliation:
Department of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. joerg.stetefeld@unibas.ch
