1nd9
From Proteopedia
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Solution Structure of the N-terminal Subdomain of Translation Initiation Factor IF2
Overview
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 betaalphaalphabetabetaalpha 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.
About this Structure
1ND9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A conserved structural motif at the N terminus of bacterial translation initiation factor IF2., Laursen BS, Mortensen KK, Sperling-Petersen HU, Hoffman DW, J Biol Chem. 2003 May 2;278(18):16320-8. Epub 2003 Feb 24. PMID:12600987
Page seeded by OCA on Tue Nov 20 22:09:22 2007
