1d1n
From Proteopedia
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 Page seeded by OCA on Fri May 2 13:20:50 2008
