Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer.
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.
Stetefeld
J
J
Department of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. joerg.stetefeld@unibas.ch
Jenny
M
M
Schulthess
T
T
Landwehr
R
R
Engel
J
J
Kammerer
R A
RA
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D019620:Desulfurococcaceae / Q000737:chemistry*; D010450:Endopeptidases / Q000378:metabolism; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D055672:Static Electricity; D014867:Water / Q000378:metabolism
D010446:Peptide Fragments; D014867:Water; D010450:Endopeptidases