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Structure of the fMet‐tRNA fMet ‐binding domain of B.stearothermophilus initiation factor IF2
Author(s) -
Meunier Sylvie,
Spurio Roberto,
Czisch Michael,
Wechselberger Rainer,
Guenneugues Marc,
Gualerzi Claudio O.,
Boelens Rolf
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.8.1918
Subject(s) - library science , biology , center (category theory) , computer science , crystallography , chemistry
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 β‐strands, connected via loops, and forms a closed β‐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·aminoacyl‐tRNA· GDP analogue have been reported and were used to propose and discuss the possible fMet‐tRNA fMet ‐binding site of IF2.