1fe6
From Proteopedia
CRYSTAL STRUCTURE OF A NATURALLY OCCURING PARALLEL RIGHT-HANDED COILED-COIL TETRAMER
Overview
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.
About this Structure
1FE6 is a Single protein structure of sequence from Staphylothermus marinus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer., Stetefeld J, Jenny M, Schulthess T, Landwehr R, Engel J, Kammerer RA, Nat Struct Biol. 2000 Sep;7(9):772-6. PMID:10966648 Page seeded by OCA on Fri May 2 16:13:30 2008
