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

FEBS Letters

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