Tunnel plasticity and quaternary structural integrity of a pentameric protein ring.
Tunnel plasticity and quaternary structural integrity of a pentameric protein ring.
复制标题
五聚体蛋白环的隧道可塑性和四级结构完整性。
DOI：
10.1110/ps.052044606
复制
发表时间：
2006
期刊：
影响因子：
--
通讯作者：
Hilvert,Donald
中科院分区：
文献类型：
--
作者：
Woycechowsky,KennethJ;Seebeck,FlorianP;Hilvert,Donald
环状蛋白低聚体在细胞中很常见。然而，蛋白质环中央隧道中的残基对整体结构完整性的重要性还没有被很好地了解。为了研究隧道位置在蛋白质组装和稳定性中的作用，我们从酿酒酵母中制备了高五聚体鲁马津合成酶(LS)的变体，其中位于隧道中间的三个残基同时发生变化。作为对称性的结果，这些突变总共导致五聚体复合体结构的15个变化。对变体的详细表征表明，它们保持了四级结构的完整性，即使在突变导致相当大的二级结构变化的情况下也是如此。因此，对称环状蛋白质的隧道，如LS，可能是蛋白质工程中一个被忽视的地方。
Cyclic protein oligomers are common in cells. However, the importance of the residues that line the central tunnel of protein rings for overall architectural integrity is not well understood. To investigate the role of tunnel positions in protein assembly and stability, we prepared variants of the homo‐pentameric lumazine synthase (LS) fromSaccharomyces cerevisiaein which the three residues that line the middle of the tunnel were simultaneously changed. As a consequence of symmetry, these mutations cause a total of 15 changes in the structure of the pentameric complex. Detailed characterization of the variants indicates that they retain quaternary structural integrity, even in cases where the mutations induce considerable secondary structure alterations. The tunnels of symmetric ring‐shaped proteins, such as LS, may consequently represent an overlooked site for protein engineering.