Conformational independence of N‐ and C‐domains in ribosomal protein L7/L12 and in the complex with protein L10
- 27 February 1998
- journal article
- Published by Wiley in FEBS Letters
- Vol. 423 (3), 347-350
- https://doi.org/10.1016/s0014-5793(98)00121-5
Abstract
Isolated N- (1–37) and C-terminal (47–120) fragments of L7 protein, and pentameric (L7) 4 L10 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) 4 L10 complex formation. The overall motions of the L7 C-domains are essentially independent both in the L7 dimer and in the (L7) 4 L10 complex. Conformational motions on a millisecond time scale are detected in the (L7) 4 L10 complex. The possible relevance of these motions to the biological function of L7/L12 is discussed.Keywords
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