Three dimensional structure of bacterial pili.
Three dimensional structure of bacterial pili.
复制标题
细菌菌毛的三维结构。
DOI：
10.1007/bf00415501
复制
发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Tainer,JA
中科院分区：
文献类型：
--
作者：
Parge,HE;McRee,DE;Capozza,MA;Bernstein,SL;Getzoff,ED;Tainer,JA
结晶学和相关的生物化学和结构的研究正在进行中的纤维形成菌毛蛋白的淋球菌菌毛。已经开发了淋球菌毛蛋白的制备规模纯化程序，该程序似乎普遍适用于细菌毛蛋白。对于三个淋球菌菌毛蛋白菌株，我们已经获得了重组菌毛纤维和三维晶体。淋球菌C30菌毛蛋白的一种针状晶体形式使用同步加速器X射线辐射衍射超过3 μ m分辨率。在这些针状晶体（晶格间距a =125.4（3）B=120.4（3），c=26.61（4）nm）上收集了分辨率为3.5 nm的衍射数据，其中菌毛蛋白亚基的堆积排列似乎类似于使用电子显微镜在菌毛纤维中看到的排列。X射线衍射数据证实了我们提出的菌毛蛋白亚基的整体多肽折叠模型，菌毛蛋白亚基是一个反平行的4-α螺旋束，类似于烟草花叶病毒外壳蛋白和肌红蛋白。
Crystallographic and associated biochemical and structural studies are in progress on the fiber-forming pilin proteins of the gonococcal pilus. Preparative scale purification procedures have been developed for the gonococcal pilin protein, which appear generally applicable to bacterial pilins. For three gonococcal pilin protein strains, we have obtained both reassembled pilus fibers and three-dimensional crystals. One needle-shaped crystal form of gonococcal C30 pilin diffracts beyond 3 Å resolution using synchrotron x-ray radiation. A diffraction data set to 3.5 Å resolution has been collected on these needle-shaped crystals (lattice spacingsa=125.4(3)b=120.4(3),c=26.61(4) Å) in which the packing arrangement of the pilin subunits appears to resemble that seen in the pilus fibers using electron microscopy. X-ray diffraction data confirm our proposed model for the overall polypeptide fold of a pilin subunit, which is an antiparallel 4-α helix bundle similar to tobacco mosaic virus coat protein and myohemerythrin.