Overall structure of yeast eIF3b-RRM.

Abstract

<p>(A) Overall fold of the yeast eIF3b-RRM showing the canonical β-α-β-β-α-β fold which at the C-terminus is followed by an extra helix which connects this domain to the rest of the protein (N- and C-termini are colored blue and red, respectively). (B) Relative orientation of two monomers in the asymmetric unit. Two monomers are held in place by interactions between residues in their β-sheets as well as the c-terminal helices. A 180° non-crystallographic symmetry axis exists between two monomers.</p

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