From Structure and Dynamics of Protein L7/L12 to Molecular Switching in Ribosome[boxs]

Based on the 1H-15N NMR spectroscopy data, the three-dimensional structure and internal dynamic properties of ribosomal protein L7 from Escherichia coli were derived. The structure of L7 dimer in solution can be described as a set of three distinct domains, tumbling rather independently and linked v...

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Bibliographic Details
Published in:The Journal of biological chemistry 2004-04, Vol.279 (17), p.17697-17706
Main Authors: Bocharov, Eduard V., Sobol, Alexander G., Pavlov, Konstantin V., Korzhnev, Dmitry M., Jaravine, Victor A., Gudkov, Anatoly T., Arseniev, Alexander S.
Format: Article
Language:English
Subjects:
Anisotropy
Crystallography, X-Ray
Dimerization
Escherichia coli - metabolism
Guanosine Triphosphate - chemistry
Hydrolysis
Magnetic Resonance Spectroscopy
Models, Molecular
Protein Binding
Protein Biosynthesis
Protein Conformation
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Ribosomal Proteins - chemistry
Ribosomes - chemistry
Ribosomes - physiology
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Summary:Based on the 1H-15N NMR spectroscopy data, the three-dimensional structure and internal dynamic properties of ribosomal protein L7 from Escherichia coli were derived. The structure of L7 dimer in solution can be described as a set of three distinct domains, tumbling rather independently and linked via flexible hinge regions. The dimeric N-terminal domain (residues 1-32) consists of two antiparallel α-α-hairpins forming a symmetrical four-helical bundle, whereas the two identical C-terminal domains (residues 52-120) adopt a compact α/β-fold. There is an indirect evidence of the existence of transitory helical structures at least in the first part (residues 33-43) of the hinge region. Combining structural data for the ribosomal protein L7/L12 from NMR spectroscopy and x-ray crystallography, it was suggested that its hinge region acts as a molecular switch, initiating “ratchet-like” motions of the L7/L12 stalk with respect to the ribosomal surface in response to elongation factor binding and GTP hydrolysis. This hypothesis allows an explanation of events observed during the translation cycle and provides useful insights into the role of protein L7/L12 in the functioning of the ribosome.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M313384200