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

ABSTRACT: 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.

SUBMITTER: Meunier S

PROVIDER: S-EPMC302012 | biostudies-literature | 2000 Apr

REPOSITORIES: biostudies-literature

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

Meunier S S Spurio R R Czisch M M Wechselberger R R Guenneugues M M Gualerzi C O CO Boelens R R

The EMBO journal 20000401 8

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 ...[more]

PMID: 10775275

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