Topology of the secondary structure elements of ribosomal protein L7/L12 from E. coli in solution

• Published in: FEBS letters 1996-02, Vol.379 (3), p.291-294
• Main Authors: Bocharov, E.V., Gudkov, A.T., Arseniev, A.S.
• Format: Article
• Language: English
• Subjects: 2D 1H-detected heteronuclear multiple quantum correlation; 2D double quantum filtered correlated spectroscopy; 2D NOE-correlated spectroscopy; 2D total correlated spectroscopy; 3 J HNα; Amino Acid Sequence; Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; C-terminal domain; CTD; DQF-COSY; Escherichia coli; Escherichia coli - chemistry; HMQC; L7/L12 protein; Molecular Sequence Data; N-terminal domain; NMR; NOE; NOESY; NTD; nuclear magnetic resonance; nuclear Overhauser enhancement; Peptide Fragments - chemistry; Peptide Fragments - isolation & purification; Protein Structure, Secondary; Ribosomal Proteins - chemistry; Ribosomal Proteins - isolation & purification; Ribosome; Ribosomes - metabolism; Secondary structure; Sequence Alignment; Sequence-specific NMR assignment; spin-spin coupling constant of HNCαH protons; the jump-and-return method of solvent signal suppression; three-dimensional; TOCSY; two-dimensional
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(95)01531-0

Topology of the secondary structure elements of ribosomal protein L7/L12 has been studied. The sequential assignment was obtained for main and side chain resonances. This allows the overall secondary structure to be described. The results of high resolution NMR studies show that dimer of the ribosomal protein L7/L12 from Escherichia coli has a parallel (head-to-head) orientation of subunits, and N-terminal domain (NTD, residues Ser1-Ser33) has no contracts with the C-terminal domain (CTD, residues Lys51-Lys120). The NMR data for CTD are in line with crystallographic structure. The flexible interdomain (hinge) region (residues Ala34-Glu50) has an unordered structure, the Pro44 forming both cis and trans peptide bonds. Due to the conformational exchange the intensities of the peaks from the NTD are low. The conformation of the NTD, which is responsible for the formation of the L7/L12 dimer, is α-helical hairpin. The NTD dimer forms an antiparallel four-α-helix bundle.