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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hatzopoulos GN,Mueller-Dieckmann Jdoi
10.1016/j.febslet.2010.01.051subject
Has Abstractpub_date
2010-03-05 00:00:00pages
1011-5issue
5eissn
0014-5793issn
1873-3468pii
S0014-5793(10)00084-0journal_volume
584pub_type
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