Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer
Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer
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DOI：
10.1038/79006
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发表时间：
2000-09-01
期刊：
影响因子：
--
通讯作者：
Kammerer, RA
中科院分区：
文献类型：
--
作者：
Stetefeld, J;Jenny, M;Kammerer, RA
来自海洋葡萄球菌 (Staphylothermus marinus) 的表层蛋白四肢蛋白 (tetrabrachion) 的多肽链片段的晶体结构已在 1.8 埃分辨率下测定。正如基于 11 个残基重复的存在所提出的，多肽链片段形成平行的右手卷曲螺旋结构。互补的疏水相互作用和复杂的表面盐桥网络形成了具有卓越性能的极其耐热的四聚体结构。与左手卷曲线圈四聚体形成鲜明对比的是，右手卷曲线圈显示出充满水分子的大疏水空腔。因此，疏水核的堆积与基于左手卷曲线圈结构设计的右手平行卷曲线圈四聚体的堆积明显不同。
The crystal structure of a polypeptide chain fragment from the surface layer protein tetrabrachion from Staphylothermus marinus has been determined at 1.8 Angstrom 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 En 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.