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Published online before print August 4, 2005, 10.1110/ps.051531305
Protein Science (2005), 14:2461-2468. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
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Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2

Hans Wienk1,4, Simona Tomaselli1,3,4, Cédric Bernard1,5, Roberto Spurio2, Delia Picone3, Claudio O. Gualerzi2 and Rolf Boelens1

1 Bijvoet Center for Biomolecular Research, Department of NMR Spectroscopy, Utrecht University, 3584 CH Utrecht, The Netherlands
2 Laboratory of Genetics, Department of Biology MCA, University of Camerino, 62032 Camerino (MC), Italy
3 Department of Chemistry, University of Napoli "Federico II," 80126 Napoli, Italy

(RECEIVED April 21, 2005; FINAL REVISION June 4, 2005; ACCEPTED June 9, 2005)

IF2 is one of three bacterial translation initiation factors that are conserved through all kingdoms of life. It binds the 30S and 50S ribosomal subunits, as well as fMet-tRNAfMet. After these interactions, fMet-tRNAfMet is oriented to the ribosomal P-site where the first amino acid of the nascent polypeptide, formylmethionine, is presented. The C-terminal domain of Bacillus stearothermophilus IF2, which is responsible for recognition and binding of fMet-tRNAfMet, contains two structured modules. Previously, the solution structure of the most C-terminal module, IF2-C2, has been elucidated by NMR spectroscopy and direct interactions between this subdomain and fMet-tRNAfMet were reported. In the present NMR study we have obtained the spectral assignment of the other module of the C-terminal domain (IF2-C1) and determined its solution structure and backbone dynamics. The IF2-C1 core forms a flattened fold consisting of a central four-stranded parallel {beta}-sheet flanked by three {alpha}-helices. Although its overall organization resembles that of subdomain III of the archaeal IF2-homolog eIF5B whose crystal structure had previously been reported, some differences of potential functional significance are evident.

Keywords: protein synthesis; translation initiation; IF2; fMet-tRNA; NMR structure

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051531305.

Reprint requests to: Rolf Boelens, Bijvoet Center for Biomolecular Research, Department of NMR Spectroscopy, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands; e-mail: r.boelens{at}chem.uu.nl; fax: +31-30-2537623.


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