Conformational independence of N‐ and C‐domains in ribosomal protein L7/L12 and in the complex with protein L10

Publisher Website
Google Scholar
Abstract
Isolated N‐ (1–37) and C‐terminal (47–120) fragments of L7 protein, and pentameric (L7)4L10 complex were studied by NMR spectroscopy in solution. The results indicate that the dimer state of the 1–37 fragment with a helical hairpin conformation is identical to the N‐terminal structure of the intact L7 dimer. The C‐terminal domain of the L7 protein does not participate in (L7)4L10 complex formation. The overall motions of the L7 C‐domains are essentially independent both in the L7 dimer and in the (L7)4L10 complex. Conformational motions on a millisecond time scale are detected in the (L7)4L10 complex. The possible relevance of these motions to the biological function of L7/L12 is discussed.