Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2.
The three-dimensional structure of the fMet-tRNA(fMet) -binding domain of translation 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-barrel similar to domain II of elongation factors EF-Tu and EF-G, despite low sequence homology. Two structures of the ternary complexes of the EF-Tu small middle dotaminoacyl-tRNA small middle dot GDP analogue have been reported and were used to propose and discuss the possible fMet-tRNA(fMet)-binding site of IF2.
Meunier
S
S
Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
Spurio
R
R
Czisch
M
M
Wechselberger
R
R
Guenneugues
M
M
Gualerzi
C O
CO
Boelens
R
R
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry; D016208:Databases, Factual; D001411:Geobacillus stearothermophilus / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010448:Peptide Initiation Factors / Q000737:chemistry*; D039881:Prokaryotic Initiation Factor-2; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012358:RNA, Transfer, Met / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D010448:Peptide Initiation Factors; D039881:Prokaryotic Initiation Factor-2; D012358:RNA, Transfer, Met