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PDBsum entry 1dd5
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of thermotoga maritima ribosome recycling factor: a tRNA mimic.
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Authors
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M.Selmer,
S.Al-Karadaghi,
G.Hirokawa,
A.Kaji,
A.Liljas.
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Ref.
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Science, 1999,
286,
2349-2352.
[DOI no: ]
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PubMed id
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Abstract
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Ribosome recycling factor (RRF), together with elongation factor G (EF-G),
catalyzes recycling of ribosomes after one round of protein synthesis. The
crystal structure of RRF was determined at 2.55 angstrom resolution. The protein
has an unusual fold where domain I is a long three-helix bundle and domain II is
a three-layer beta/alpha/beta sandwich. The molecule superimposes almost
perfectly with a transfer RNA (tRNA) except that the amino acid-binding 3' end
is missing. The mimicry suggests that RRF interacts with the posttermination
ribosomal complex in a similar manner to a tRNA, leading to disassembly of the
complex. The structural arrangement of this mimicry is entirely different from
that of other cases of less pronounced mimicry of tRNA so far described.
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Figure 1.
Fig. 1. (A) A portion of the 2.9 Å MAD map after DM
contoured at 1.0  with O
(34) superimposed on residue 4-24 (H1, left) and 157-176 (H6,
right) of the final refined model. (B) Molmol (34) ribbon
representation of RRF. The chain starts from domain I (green),
then goes through domain II (red) and back to domain I (blue).
The conserved and conservatively substituted amino acids are
marked with orange (all known sequences) and yellow (for
bacteria and chloroplast).
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Figure 3.
Fig. 3. (A) Stereo ribbon representation of the superposition
of RRF (blue) and yeast tRNA^Phe (red) with Molmol (34). (B)
Comparison of EF-G (36) and the ternary complex of EF-Tu + GDPNP
+ aatRNA (32). EF-G (left) is similar in shape to EF-Tu + GDPNP
+ aatRNA (right). Domain III-IV of EF-G (purple) imitates the
shape of the tRNA (red) bound to EF-Tu (yellow). The remaining
domains of EF-G (green) are structurally similar to EF-Tu. RRF
(A) imitates the tRNA in a totally different manner. (C) Grasp
(34) surface representation of the superposition of RRF (blue)
and yeast tRNA^Phe (red). The shapes and sizes of the surfaces
are nearly identical except for the acceptor end of tRNA (to the
right), which has no corresponding part in RRF.
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The above figures are
reprinted
by permission from the AAAs:
Science
(1999,
286,
2349-2352)
copyright 1999.
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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray analysis of thermotoga maritima ribosome recycling factor.
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Authors
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M.Selmer,
S.Al-Karadaghi,
G.Hirokawa,
A.Kaji,
A.Liljas.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1999,
55,
2049-2050.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1 Native crystal of T. maritima ribosome recycling
factor. The bipyramidal crystal has approximate dimensions 0.3 ×
0.3 × 0.5 mm.
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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Secondary reference #2
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Title
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Cloning and overexpression of thermotoga maritima rrf
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Authors
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K.Atarashi,
A.Kaji.
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Ref.
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TO BE PUBLISHED ...
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