FEBS Letters | |
Conformational independence of N‐ and C‐domains in ribosomal protein L7/L12 and in the complex with protein L10 | |
Arseniev, A.S2  Gudkov, A.T1  Bocharov, E.V2  Budovskaya, E.V1  | |
[1] Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia;Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16/10, Moscow 117871, Russia | |
关键词: Ribosome; L7/L12 protein; L10 protein; L7-L10 complex; Nuclear magnetic resonance; Structure; 2D; two-dimensional; NOE; nuclear Overhauser enhancement; NOESY; 2D NOE-correlated spectroscopy; TOCSY; 2D total correlated spectroscopy; HSQC and HMQC; 2D 1H-detected heteronuclear single and multiple quantum correlation; jr; the jump-and-return method of solvent signal suppression; | |
DOI : 10.1016/S0014-5793(98)00121-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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RO201912020305618ZK.pdf | 262KB | download |