Structural highlights
Function
[IF1_MYCTU] No specific function has so far been attributed to this initiation factor; however, it seems to stimulate more or less all the activities of the other two initiation factors, IF-2 and IF-3 (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of translation initiation factor 1 from Mycobacterium tuberculosis and inferred binding to the 30S ribosomal subunit.,Hatzopoulos GN, Mueller-Dieckmann J FEBS Lett. 2010 Mar 5;584(5):1011-5. Epub 2010 Feb 2. PMID:20132820[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hatzopoulos GN, Mueller-Dieckmann J. Structure of translation initiation factor 1 from Mycobacterium tuberculosis and inferred binding to the 30S ribosomal subunit. FEBS Lett. 2010 Mar 5;584(5):1011-5. Epub 2010 Feb 2. PMID:20132820 doi:10.1016/j.febslet.2010.01.051
