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Originally published In Press as doi:10.1074/jbc.M212960200 on February 24, 2003

J. Biol. Chem., Vol. 278, Issue 18, 16320-16328, May 2, 2003
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A Conserved Structural Motif at the N Terminus of Bacterial Translation Initiation Factor IF2*

Brian Søgaard LaursenDagger §, Kim Kusk MortensenDagger , Hans Uffe Sperling-PetersenDagger , and David W. Hoffman||**

From the Dagger  Department of Molecular Biology, University of Aarhus, DK8000 Aarhus, Denmark and the || Department of Chemistry and Biochemistry, Institute for Cellular and Molecular Biology, University of Texas, Austin, Texas 78712

The 18-kDa Domain I from the N-terminal region of translation initiation factor IF2 from Escherichia coli was expressed, purified, and structurally characterized using multidimensional NMR methods. Residues 2-50 were found to form a compact subdomain containing three short beta -strands and three alpha -helices, folded to form a beta alpha alpha beta beta alpha motif with the three helices packed on the same side of a small twisted beta -sheet. The hydrophobic amino acids in the core of the subdomain are conserved in a wide range of species, indicating that a similarly structured motif is present at the N terminus of IF2 in many of the bacteria. External to the compact 50-amino acid subdomain, residues 51-97 are less conserved and do not appear to form a regular structure, whereas residues 98-157 form a helix containing a repetitive sequence of mostly hydrophilic amino acids. Nitrogen-15 relaxation rate measurements provide evidence that the first 50 residues form a well ordered subdomain, whereas other regions of Domain I are significantly more mobile. The compact subdomain at the N terminus of IF2 shows structural homology to the tRNA anticodon stem contact fold domains of the methionyl-tRNA and glutaminyl-tRNA synthetases, and a similar fold is also found in the B5 domain of the phenylalanine-tRNA synthetase. The results of the present work will provide guidance for the design of future experiments directed toward understanding the functional roles of this widely conserved structural domain within IF2.

* This work was funded by Grants 9901722 and 51-00-0263 from the Familien Hede Nielsens Fund and the Danish Natural Science Research Council (to H. U. S.-P.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Chemical shift assignments for the domain of IF2 have been submitted to the BioMagResBank and assigned the accession number BMRB-5624.

The atomic coordinates and the structure factors (code 1ND9) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

§ Supported by a personal grant from Knud Højgaards Fund, Denmark.

To whom correspondence may be addressed: Dept. of Molecular Biology, University of Aarhus, Denmark. Tel.: 45-89425050; Fax: 45-86182812; E-mail: husp@biobase.dk.

** Supported by Grant F-1353 from the Welch Foundation. To whom correspondence may be addressed: Dept. of Chemistry and Biochemistry, Institute for Cellular and Molecular Biology, University of Texas, Austin, TX 78712. Tel.: 512-471-7859; Fax: 512-471-8696; E-mail: dhoffman@mail.utexas.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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