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Structure of translation initiation factor 1 from Mycobacterium tuberculosis and inferred binding to the 30S ribosomal subunit
Author(s) -
Hatzopoulos Georgios N.,
Mueller-Dieckmann Jochen
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.01.051
Subject(s) - thermus thermophilus , 30s , protein subunit , mycobacterium tuberculosis , ribosomal rna , ribosomal protein , crystal structure , eukaryotic small ribosomal subunit , initiation factor , chemistry , structure function , crystallography , ribosome , biology , physics , tuberculosis , biochemistry , rna , medicine , escherichia coli , particle physics , pathology , gene
The crystal structure of the free form of IF1 from Mycobacterium tuberculosis has been determined at 1.47 Å 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.