Journal
FEBS LETTERS
Volume 584, Issue 5, Pages 1011-1015Publisher
WILEY
DOI: 10.1016/j.febslet.2010.01.051
Keywords
Prokaryotic initiation factor-1; X-ray structure; Mycobacterium tuberculosis H37Rv
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The crystal structure of the free form of IF1 from Mycobacterium tuberculosis has been determined at 1.47 angstrom resolution. The structure adopts the expected OB fold and matches the high structural conservation among IF1 orthologues. In order to further explore the function of Mtb-IF1, we built a model of its interaction with the 30S ribosomal subunit based on the crystal structure of the complex from Thermus thermophilus. The model suggests that several functionally important side chain residues undergo large movements while the rest of the protein in complex shows only very limited conformational change as compared to its form in solution. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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