3I4O
Crystal Structure of Translation Initiation Factor 1 from Mycobacterium tuberculosis
Summary for 3I4O
Entry DOI | 10.2210/pdb3i4o/pdb |
Descriptor | Translation initiation factor IF-1 (2 entities in total) |
Functional Keywords | translation initiation, if1, initiation factor, protein biosynthesis, translation |
Biological source | Mycobacterium tuberculosis |
Total number of polymer chains | 2 |
Total formula weight | 18271.29 |
Authors | Hatzopoulos, G.N.,Mueller-Dieckmann, J. (deposition date: 2009-07-02, release date: 2010-02-23, Last modification date: 2024-03-20) |
Primary citation | Hatzopoulos, G.N.,Mueller-Dieckmann, J. Structure of translation initiation factor 1 from Mycobacterium tuberculosis and inferred binding to the 30S ribosomal subunit. Febs Lett., 584:1011-1015, 2010 Cited by PubMed Abstract: The crystal structure of the free form of IF1 from Mycobacterium tuberculosis has been determined at 1.47 A 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. PubMed: 20132820DOI: 10.1016/j.febslet.2010.01.051 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.47 Å) |
Structure validation
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