The flexible region of protein L12 from bacterial ribosomes studied by proton nuclear magnetic resonance.
The dimeric protein L7/L12 from bacterial ribosomes has a highly elongated and flexible structure. We have, using 1H NMR methods, analyzed the extent of the flexible region and also the size of the organized structures of the molecule. A number of mutants of the protein as well as monomeric and dimeric forms of the protein and a COOH-terminal fragment have been used for the identification of certain resonances. Thus, residues 37-50 were found to be highly mobile whereas the amino-terminal and COOH-terminal regions are organized into folded domains. The flexibility between the domains and its relation to functional properties of the protein are discussed.
Bushuev
V N
VN
Institute of Experimental Cardiology, Academy of Medical Sciences, Moscow.
Gudkov
A T
AT
Liljas
A
A
Sepetov
N F
NF
D000107:Acetylation; D000409:Alanine; D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D004926:Escherichia coli / Q000032:analysis; D005998:Glycine; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009154:Mutation; D011392:Proline; D011487:Protein Conformation; D012269:Ribosomal Proteins / Q000235:genetics; D014633:Valine
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D012269:Ribosomal Proteins; C016700:ribosomal protein L7-L12; D011392:Proline; D014633:Valine; D000409:Alanine; D005998:Glycine