Pellecchia M, Sebbel P, Hermanns U, Wüthrich K, Glockshuber R
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Hönggerberg, Zürich, Switzerland.
Nat Struct Biol. 1999 Apr;6(4):336-9. doi: 10.1038/7573.
The 23 kDa two-domain periplasmic chaperone FimC from Escherichia coli is required for the assembly of type-1 pili, which are filamentous, highly oligomeric protein complexes anchored to the outer bacterial membrane that mediate adhesion of pathogenic E. coli strains to host cell surfaces. Here we identified the contact sites on the surface of the NMR structure of FimC that are responsible for the binding of the 28 kDa mannose-binding type-1 pilus subunit FimH by 15N and 1H NMR chemical shift mapping, using transverse relaxation-optimized spectroscopy (TROSY). The FimH-binding surface of FimC is formed nearly entirely by the N-terminal domain, and its extent and shape indicate that FimC binds a folded form of the pilus subunits.
来自大肠杆菌的23 kDa双结构域周质伴侣蛋白FimC是1型菌毛组装所必需的，1型菌毛是锚定在细菌外膜上的丝状、高度寡聚的蛋白质复合物，介导致病性大肠杆菌菌株与宿主细胞表面的粘附。在这里，我们使用横向弛豫优化光谱法（TROSY），通过15N和1H NMR化学位移映射，确定了FimC的NMR结构表面上负责与28 kDa甘露糖结合型1型菌毛亚基FimH结合的接触位点。FimC的FimH结合表面几乎完全由N端结构域形成，其范围和形状表明FimC结合菌毛亚基的折叠形式。
