<h2>Summary</h2> The L7/12 stalk of the large subunit of bacterial ribosomes encompasses protein L10 and multiple copies of L7/12. We present crystal structures of <i>Thermotoga maritima</i> L10 in complex with three L7/12 N-terminal-domain dimers, refine the structure of an archaeal L10E N-terminal domain on the 50S subunit, and identify these elements in cryo-electron-microscopic reconstructions of <i>Escherichia coli</i> ribosomes. The mobile C-terminal helix α8 of L10 carries three L7/12 dimers in <i>T. maritima</i> and two in <i>E. coli,</i> in concordance with the different length of helix α8 of L10 in these organisms. The stalk is organized into three elements (stalk base, L10 helix α8-L7/12 N-terminal-domain complex, and L7/12 C-terminal domains) linked by flexible connections. Highly mobile L7/12 C-terminal domains promote recruitment of translation factors to the ribosome and stimulate GTP hydrolysis by the ribosome bound factors through stabilization of their active GTPase conformation.

Structural Basis for the Function of the Ribosomal L7/12 Stalk in Factor Binding and GTPase Activation

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