1d1n

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1d1n

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SOLUTION STRUCTURE OF THE FMET-TRNAFMET BINDING DOMAIN OF BECILLUS STEAROTHERMOPHILLUS TRANSLATION INITIATION FACTOR IF2

Overview

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.

About this Structure

1D1N is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

Reference

Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2., Meunier S, Spurio R, Czisch M, Wechselberger R, Guenneugues M, Gualerzi CO, Boelens R, EMBO J. 2000 Apr 17;19(8):1918-26. PMID:10775275

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