Journal
CELL
Volume 121, Issue 7, Pages 991-1004Publisher
CELL PRESS
DOI: 10.1016/j.cell.2005.04.015
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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 Thermotoga maritima L10 in complex with three L7/12 N-terminaldomain 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 Escherichia coli ribosomes. The mobile C-terminal helix alpha 8 of L10 carries three L7/12 dimers in T maritima and two in E. coli, in concordance with the different length of helix alpha 8 of L10 in these organisms. The stalk is organized into three elements (stalk base, L10 helix alpha 8-L7/12 N-terminaldomain 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.
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