Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer

Jörg Stetefeld, Margrit Jenny, Therese Schulthess, Ruth Landwehr, Jürgen Engel, Richard A. Kammerer

    Research output: Contribution to journalArticlepeer-review


    The crystal structure of a polypeptide chain fragment from the surface layer protein tetrabrachion from Staphylothermus marinus has been determined at 1.8 Å 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.
    Original languageEnglish
    Pages (from-to)772-776
    Number of pages4
    JournalNature Structural Biology
    Issue number9
    Publication statusPublished - Sept 2000


    Dive into the research topics of 'Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer'. Together they form a unique fingerprint.

    Cite this