Tetrameric coiled coil domain of Sendai virus phosphoprotein.
The high resolution X-ray structure of the Sendai virus oligomerization domain reveals a homotetrameric coiled coil structure with many details that are different from classic coiled coils with canonical hydrophobic heptad repeats. Alternatives to the classic knobs-into-holes packing lead to differences in supercoil pitch and diameter that allow water molecules inside the core. This open and more hydrophilic structure does not seem to be destabilized by mutations that would be expected to disrupt classic coiled coils.
Tarbouriech
N
N
European Synchrotron Radiation Facility, Grenoble cedex, France.
Curran
J
J
Ruigrok
R W
RW
Burmeister
W P
WP
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D018108:Respirovirus / Q000737:chemistry*; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism*
C055859:P protein, Sendai virus; D010446:Peptide Fragments; D010750:Phosphoproteins; D014764:Viral Proteins