Structure of the fMet-tRNAfMet-binding domain of B.stearothermophilus initiation factor IF2
- 17 April 2000
- journal article
- Published by Springer Nature in The EMBO Journal
- Vol. 19 (8) , 1918-1926
- https://doi.org/10.1093/emboj/19.8.1918
Abstract
The three‐dimensional structure of the fMet‐tRNAfMet‐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‐tRNAfMet‐binding site of IF2.Keywords
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