1FE6

CRYSTAL STRUCTURE OF A NATURALLY OCCURING PARALLEL RIGHT-HANDED COILED-COIL TETRAMER

1FE6 の概要

• エントリーDOI: 10.2210/pdb1fe6/pdb
• 分子名称: TETRABRACHION (2 entities in total)
• 機能のキーワード: right handed coiled coil, protein binding
• 由来する生物種: Staphylothermus marinus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 23370.46

構造登録者

Stetefeld, J. (登録日: 2000-07-21, 公開日: 2001-01-21, 最終更新日: 2024-02-07)

主引用文献

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

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: 10966648
DOI: 10.1038/79006

実験手法

X-RAY DIFFRACTION (1.8 Å)