1FE6
CRYSTAL STRUCTURE OF A NATURALLY OCCURING PARALLEL RIGHT-HANDED COILED-COIL TETRAMER
Summary for 1FE6
| Entry DOI | 10.2210/pdb1fe6/pdb |
| Descriptor | TETRABRACHION (2 entities in total) |
| Functional Keywords | right handed coiled coil, protein binding |
| Biological source | Staphylothermus marinus |
| Total number of polymer chains | 4 |
| Total formula weight | 23370.46 |
| Authors | Stetefeld, J. (deposition date: 2000-07-21, release date: 2001-01-21, Last modification date: 2024-02-07) |
| Primary citation | Stetefeld, J.,Jenny, M.,Schulthess, T.,Landwehr, R.,Engel, J.,Kammerer, R.A. Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer. Nat.Struct.Biol., 7:772-776, 2000 Cited by 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. PubMed: 10966648DOI: 10.1038/79006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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