Conformational independence of N- and C-domains in ribosomal protein L7/L12 and in the complex with protein L10.
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.
Bocharov
E V
EV
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow.
Gudkov
A T
AT
Budovskaya
E V
EV
Arseniev
A S
AS
D000595:Amino Acid Sequence; D019281:Dimerization; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D014176:Protein Biosynthesis / Q000235:genetics; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D000080882:Ribosomal Protein L10; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000378:metabolism
D029968:Escherichia coli Proteins; D010446:Peptide Fragments; D012269:Ribosomal Proteins; C512844:rplL protein, E coli