Ribosome anti-association factor elF6 (originally named according to transl
ation initiation terminology as eukaryotic initiation factor 6) binds to th
e large ribosomal subunit, thereby preventing inappropriate interactions wi
th the small subunit during initiation of protein synthesis. We have determ
ined the X-ray structures of two IF6 homologs, Methanococcus jannaschii arc
haeal alF6 and Sacchromyces cerevisiae elF6, revealing a phylogenetically c
onserved 25 kDa protein consisting of five quasi identical alpha/beta subdo
mains arrayed about a five-fold axis of pseudosymmetry. Yeast elF6 prevents
ribosomal subunit association. Comparative protein structure modeling with
other known archaeal and eukaryotic homologs demonstrated the presence of
two conserved surface regions, one or both of which may bind the large ribo
somal subunit.