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PDBsum entry 1zb4
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Structural protein
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PDB id
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1zb4
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References listed in PDB file
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Key reference
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Title
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Structural basis for the function of the ribosomal l7/12 stalk in factor binding and gtpase activation.
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Authors
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M.Diaconu,
U.Kothe,
F.Schlünzen,
N.Fischer,
J.M.Harms,
A.G.Tonevitsky,
H.Stark,
M.V.Rodnina,
M.C.Wahl.
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Ref.
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Cell, 2005,
121,
991.
[DOI no: ]
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PubMed id
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Abstract
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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-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.
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Figure 3.
Figure 3. Details of the L10-L12 Interaction
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Figure 6.
Figure 6. Functional Role of L12
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2005,
121,
991-0)
copyright 2005.
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