Structure of the fMet-tRNA(fMet)-binding domain of B.stearothermophilus initiation factor IF2

Authors
Meunier, S Spurio, R Czisch, M Wechselberger, R Guenneugues, M Gualerzi, CO Boelens, R
Citation
S. Meunier et al., Structure of the fMet-tRNA(fMet)-binding domain of B.stearothermophilus initiation factor IF2, EMBO J, 19(8), 2000, pp. 1918-1926
Citations number
52
Categorie Soggetti
Molecular Biology & Genetics
Journal title
EMBO JOURNAL
ISSN journal
02614189 → ACNP
Volume
19
Issue
8
Year of publication
2000
Pages
1918 - 1926
Database
ISI
SICI code
0261-4189(20000417)19:8<1918:SOTFDO>2.0.ZU;2-G
Abstract
The three-dimensional structure of the fMet-tRNA(fMet) -binding domain of t ranslation initiation factor IF2 from Bacillus stearothermophilus has been determined by heteronuclear NMR spectroscopy. Its structure consists of six antiparallel beta-strands, connected via loops, and forms a closed beta-ba rrel similar to domain II of elongation factors EF-Tu and EF-F, despite low sequence homology. Two structures of the ternary complexes of the EF-Tu.am inoacyl-tRNA. GDP analogue have been reported and were used to propose and discuss the possible fMet-tRNA(fMet)-binding site of IF2.