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J. Biol. Chem., Vol. 279, Issue 17, 17697-17706, April 23, 2004

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From Structure and Dynamics of Protein L7/L12 to Molecular Switching in Ribosome^*

Eduard V. Bocharov, Alexander G. Sobol, Konstantin V. Pavlov¶, Dmitry M. Korzhnev||, Victor A. Jaravine, Anatoly T. Gudkov**, and Alexander S. Arseniev

From the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16/10, Moscow 117997, Russia, ^¶Frumkin Institute of Electrochemistry, Russian Academy of Science, Moscow 117071, Russia, ^||Department Medical Genetics, University of Toronto, Toronto, Ontario M5S 1A8, Canada, and ^**Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russia

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 --hairpins forming a symmetrical four-helical bundle, whereas the two identical C-terminal domains (residues 52-120) adopt a compact /-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.

Received for publication, December 8, 2003 , and in revised form, February 4, 2004.

The atomic coordinates and structure factors (codes 1RQU, 1RQV, 1RQT, and 1RQS) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by grants from the Program RAS MCB and the Ministry of Science and Technology of Russian Federation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental data and Supplemental Figs. 1-3.

Recipient of support from K. A. Beirit. To whom correspondence may be addressed. Tel.: 7(095)-330-7483; Fax: 7(095)-335-5033; E-mail: bon{at}nmr.ru.

To whom correspondence may be addressed. Tel.: 7(095)-330-5929; Fax: 7(095)-335-5033; E-mail: aars{at}nmr.ru.

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