1z9b | pdb_00001z9b
Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2
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Overview
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-tRNAf(Met). After these interactions, fMet-tRNAf(Met) 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-tRNAf(Met), 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-tRNAf(Met) 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.
About this Structure
1Z9B is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2., Wienk H, Tomaselli S, Bernard C, Spurio R, Picone D, Gualerzi CO, Boelens R, Protein Sci. 2005 Sep;14(9):2461-8. Epub 2005 Aug 4. PMID:16081655
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