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Papers In Press, published online ahead of print February 11, 2004
NMR, Russian Academy of Sciences, Moscow, Moscow 117997
Corresponding Author: aars{at}nmr.ru
Based on the 1H-15N NMR spectroscopy data the three-dimensional structure and internal dynamic properties of ribosomal protein L7 from E. 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 alfa-alfa-hairpins forming a symmetrical four-helical bundle, whereas the two identical C-terminal domains (residues 52-120) adopt a compact alfa/beta 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 explaining events observed during the translation cycle and provides useful insights into the role of protein L7/L12 in the functioning of the ribosome
J. Biol. Chem, 10.1074/jbc.M313384200
Submitted on December 8, 2003
Revised on February 4, 2004
Accepted on February 10, 2004
From structure and dynamics of protein L7/L12 to molecular switching in ribosome
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