1ZAV

Ribosomal Protein L10-L12(NTD) Complex, Space Group P21

Summary for 1ZAV

• Entry DOI: 10.2210/pdb1zav/pdb
• Related: 1ZAW 1ZAX 1ZB4
• Descriptor: 50S ribosomal protein L10, 50S ribosomal protein L7/L12 (3 entities in total)
• Functional Keywords: ribosome structure and function, l10-l12 complex structure, l10e structure, l7/12 ribosomal stalk, thiostrepton loop of 23s rrna, translation factor recruitment, gtpase stimulation, mechanism of translation, rapid kinetics, structural protein
• Biological source: Thermotoga maritima; More
• Total number of polymer chains: 7
• Total formula weight: 40896.79

Authors

Diaconu, M.,Kothe, U.,Schluenzen, F.,Fischer, N.,Harms, J.M.,Tonevitski, A.G.,Stark, H.,Rodnina, M.V.,Wahl, M.C. (deposition date: 2005-04-07, release date: 2005-07-12, Last modification date: 2024-02-14)

Primary citation

Diaconu, M.,Kothe, U.,Schluenzen, F.,Fischer, N.,Harms, J.M.,Tonevitski, A.G.,Stark, H.,Rodnina, M.V.,Wahl, M.C.
Structural Basis for the Function of the Ribosomal L7/12 Stalk in Factor Binding and GTPase Activation.
Cell(Cambridge,Mass.), 121:991-1004, 2005

PubMed Abstract: 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-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 Escherichia coli ribosomes. The mobile C-terminal helix alpha8 of L10 carries three L7/12 dimers in T. maritima and two in E. coli, in concordance with the different length of helix alpha8 of L10 in these organisms. The stalk is organized into three elements (stalk base, L10 helix alpha8-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.

PubMed: 15989950
DOI: 10.1016/j.cell.2005.04.015

Experimental method

X-RAY DIFFRACTION (1.9 Å)