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

The three-dimensional structure of the fMet-tRNA super(fMet) - binding domain of translation initiation factor IF2 from Bacillus stearothermophilus has been determined by heteronuclear NMR spectroscopy. Its structure consists of six antiparallel s-strands, connected via loops, and forms a closed s-...

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Bibliographic Details
Published in:	The EMBO journal Vol. 19; no. 8; pp. 1918 - 1926
Main Authors:	Meunier, S, Spurio, R, Czisch, M, Wechselberger, R, Guenneugues, M, Gualerzi, C, Boelens, R
Format:	Journal Article
Language:	English
Published:	17-04-2000
Subjects:	Bacillus stearothermophilus tRNA fMet
Online Access:	Get full text
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Summary:	The three-dimensional structure of the fMet-tRNA super(fMet) - binding domain of translation initiation factor IF2 from Bacillus stearothermophilus has been determined by heteronuclear NMR spectroscopy. Its structure consists of six antiparallel s-strands, connected via loops, and forms a closed s- 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 super(fMet)-binding site of IF2.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 content type line 23 ObjectType-Feature-1
ISSN:	0261-4189