|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
94 a.a.*
|
 |
|
|
|
|
|
|
|
267 a.a.*
|
 |
|
|
|
|
|
|
|
209 a.a.*
|
 |
|
|
|
|
|
|
|
201 a.a.*
|
 |
|
|
|
|
|
|
|
178 a.a.*
|
 |
|
|
|
|
|
|
|
176 a.a.*
|
 |
|
|
|
|
|
|
|
140 a.a.*
|
 |
|
|
|
|
|
|
|
121 a.a.*
|
 |
|
|
|
|
|
|
|
144 a.a.*
|
 |
|
|
|
|
|
|
|
136 a.a.*
|
 |
|
|
|
|
|
|
|
127 a.a.*
|
 |
|
|
|
|
|
|
|
117 a.a.*
|
 |
|
|
|
|
|
|
|
114 a.a.*
|
 |
|
|
|
|
|
|
|
117 a.a.*
|
 |
|
|
|
|
|
|
|
103 a.a.*
|
 |
|
|
|
|
|
|
|
110 a.a.*
|
 |
|
|
|
|
|
|
|
99 a.a.*
|
 |
|
|
|
|
|
|
|
102 a.a.*
|
 |
|
|
|
|
|
|
|
84 a.a.*
|
 |
|
|
|
|
|
|
|
63 a.a.*
|
 |
|
|
|
|
|
|
|
58 a.a.*
|
 |
|
|
|
|
|
|
|
70 a.a.*
|
 |
|
|
|
|
|
|
|
56 a.a.*
|
 |
|
|
|
|
|
|
|
54 a.a.*
|
 |
|
|
|
|
|
|
|
46 a.a.*
|
 |
|
|
|
|
|
|
|
64 a.a.*
|
 |
|
|
|
|
|
|
|
38 a.a.*
|
 |
|
|
|
|
|
|
|
141 a.a.*
|
 |
|
|
|
|
|
|
|
149 a.a.*
|
 |
|
|
|
|
|
|
|
223 a.a.*
|
 |
|
|
|
|
|
|
|
684 a.a.*
|
 |
|
|
|
|
|
|
|
185 a.a.*
|
 |
|
|
|
|
|
|
* Residue conservation analysis
|
|
* C-alpha coords only
|
|
|
|
|
PDB id:
|
 |
|
 |
| Name: |
 |
Ribosome
|
 |
|
Title:
|
 |
50s subunit with ef-g(gdpnp) and rrf bound
|
|
Structure:
|
 |
5s ribosomal RNA. Chain: a. 23s ribosomal RNA. Chain: b. 50s ribosomal protein l25. Chain: v. 50s ribosomal protein l2. Chain: c. 50s ribosomal protein l3.
|
|
Source:
|
 |
Escherichia coli. Organism_taxid: 562. Organism_taxid: 562
|
|
Authors:
|
 |
N.Gao,A.V.Zavialov,M.Ehrenberg,J.Frank
|
Key ref:
|
 |
N.Gao
et al.
(2007).
Specific interaction between EF-G and RRF and its implication for GTP-dependent ribosome splitting into subunits.
J Mol Biol,
374,
1345-1358.
PubMed id:
DOI:
|
 |
|
Date:
|
 |
|
24-Sep-07
|
Release date:
|
04-Mar-08
|
|
|
|
|
|
|
Headers
|
 |
|
|
References
|
|
|
|
|
|
|
P68919
(RL25_ECOLI) -
Large ribosomal subunit protein bL25 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
94 a.a.
94 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P60422
(RL2_ECOLI) -
Large ribosomal subunit protein uL2 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
273 a.a.
267 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P60438
(RL3_ECOLI) -
Large ribosomal subunit protein uL3 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
209 a.a.
209 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P60723
(RL4_ECOLI) -
Large ribosomal subunit protein uL4 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
201 a.a.
201 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P62399
(RL5_ECOLI) -
Large ribosomal subunit protein uL5 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
179 a.a.
178 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0AG55
(RL6_ECOLI) -
Large ribosomal subunit protein uL6 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
177 a.a.
176 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0AA10
(RL13_ECOLI) -
Large ribosomal subunit protein uL13 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
142 a.a.
140 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0ADY3
(RL14_ECOLI) -
Large ribosomal subunit protein uL14 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
123 a.a.
121 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P02413
(RL15_ECOLI) -
Large ribosomal subunit protein uL15 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
144 a.a.
144 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0ADY7
(RL16_ECOLI) -
Large ribosomal subunit protein uL16 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
136 a.a.
136 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0AG44
(RL17_ECOLI) -
Large ribosomal subunit protein bL17 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
127 a.a.
127 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0C018
(RL18_ECOLI) -
Large ribosomal subunit protein uL18 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
117 a.a.
117 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0A7K6
(RL19_ECOLI) -
Large ribosomal subunit protein bL19 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
115 a.a.
114 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0A7L3
(RL20_ECOLI) -
Large ribosomal subunit protein bL20 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
118 a.a.
117 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0AG48
(RL21_ECOLI) -
Large ribosomal subunit protein bL21 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
103 a.a.
103 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P61175
(RL22_ECOLI) -
Large ribosomal subunit protein uL22 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
110 a.a.
110 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0ADZ0
(RL23_ECOLI) -
Large ribosomal subunit protein uL23 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
100 a.a.
99 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P60624
(RL24_ECOLI) -
Large ribosomal subunit protein uL24 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
104 a.a.
102 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0A7L8
(RL27_ECOLI) -
Large ribosomal subunit protein bL27 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
85 a.a.
84 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0A7M6
(RL29_ECOLI) -
Large ribosomal subunit protein uL29 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
63 a.a.
63 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0AG51
(RL30_ECOLI) -
Large ribosomal subunit protein uL30 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
59 a.a.
58 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0A7M9
(RL31_ECOLI) -
Large ribosomal subunit protein bL31 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
70 a.a.
70 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0A7N4
(RL32_ECOLI) -
Large ribosomal subunit protein bL32 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
57 a.a.
56 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0A7N9
(RL33_ECOLI) -
Large ribosomal subunit protein bL33 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
55 a.a.
54 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0A7P5
(RL34_ECOLI) -
Large ribosomal subunit protein bL34 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
46 a.a.
46 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0A7Q1
(RL35_ECOLI) -
Large ribosomal subunit protein bL35 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
65 a.a.
64 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0A7Q6
(RL36_ECOLI) -
Large ribosomal subunit protein bL36A from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
38 a.a.
38 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0A7J7
(RL11_ECOLI) -
Large ribosomal subunit protein uL11 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
142 a.a.
141 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0A7R1
(RL9_ECOLI) -
Large ribosomal subunit protein bL9 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
149 a.a.
149 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
P0A7L0
(RL1_ECOLI) -
Large ribosomal subunit protein uL1 from Escherichia coli (strain K12)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
234 a.a.
223 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
 |
|
|
 |
 |
 |
 |
Enzyme class 2:
|
 |
Chains V, C, D, E, F, G, J, K, L, M, N, O, P, Q, R, S, T, U, W, X, Y, Z, 0, 1, 2, 3, 4, I, H, 9, 8:
E.C.?
|
|
 |
 |
 |
 |
 |
Enzyme class 3:
|
 |
Chain 7:
E.C.3.6.5.-
- ?????
|
|
 |
 |
 |
 |
 |
 |
 |
|
Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
DOI no:
|
J Mol Biol
374:1345-1358
(2007)
|
|
PubMed id:
|
|
|
|
|
| |
|
Specific interaction between EF-G and RRF and its implication for GTP-dependent ribosome splitting into subunits.
|
|
N.Gao,
A.V.Zavialov,
M.Ehrenberg,
J.Frank.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
After termination of protein synthesis, the bacterial ribosome is split into its
30S and 50S subunits by the action of ribosome recycling factor (RRF) and
elongation factor G (EF-G) in a guanosine 5'-triphosphate
(GTP)-hydrolysis-dependent manner. Based on a previous cryo-electron microscopy
study of ribosomal complexes, we have proposed that the binding of EF-G to an
RRF-containing posttermination ribosome triggers an interdomain rotation of RRF,
which destabilizes two strong intersubunit bridges (B2a and B3) and, ultimately,
separates the two subunits. Here, we present a 9-A (Fourier shell correlation
cutoff of 0.5) cryo-electron microscopy map of a 50S x EF-G x guanosine
5'-[(betagamma)-imido]triphosphate x RRF complex and a quasi-atomic model
derived from it, showing the interaction between EF-G and RRF on the 50S subunit
in the presence of the noncleavable GTP analogue guanosine
5'-[(betagamma)-imido]triphosphate. The detailed information in this model and a
comparative analysis of EF-G structures in various nucleotide- and
ribosome-bound states show how rotation of the RRF head domain may be triggered
by various domains of EF-G. For validation of our structural model, all known
mutations in EF-G and RRF that relate to ribosome recycling have been taken into
account. More importantly, our results indicate a substantial conformational
change in the Switch I region of EF-G, suggesting that a conformational signal
transduction mechanism, similar to that employed in transfer RNA translocation
on the ribosome by EF-G, translates a large-scale movement of EF-G's domain IV,
induced by GTP hydrolysis, into the domain rotation of RRF that eventually
splits the ribosome into subunits.
|
|
|
|
|
| |
Selected figure(s)
|
|
|
| |
 |
 |
|
 |
|
 |
Figure 1.
Fig. 1. Overview of the quasi-atomic model of the
50S·EF-G·GDPNP·RRF complex. (a) Stereo view
of the quasi-atomic structure of the
50S·EF-G·GDPNP·RRF complex superimposed
with the cryo-EM density map. (b) The same stereo view of the
quasi-atomic structure only. (c) Surface representation of the
cryo-EM density map. (d) Overview of the interactions between
EF-G and RRF. Ribosomal proteins, rRNAs, EF-G, and RRF are
painted in green, gray, red, and blue, respectively. The domains
of EF-G are labeled as I–IV. The two domains of RRF are
labeled as “tail” (domain I) and “head” (domain II).
Landmarks: L7L12, L7/12 stalk; L1, L1 stalk; CP, central
protuberance; arc, arc-like connection between EF-G and L7/L12
stalk base.
|
 |
Figure 2.
Fig. 2. Interactions between EF-G domain III and the
interdomain hinges of RRF. (a) The interactions between one loop
of EF-G domain III (Lys422-Lys424) and one of the hinges
(Thr106-Glu108) of RRF. (b) Interactions between the other loop
of EF-G domain III (Glu450-Asn453) and the two hinges and their
neighboring residues of RRF. The residue stretches participating
in the interactions are painted in green and yellow for RRF and
EF-G, respectively. Residues that involve very strong contacts
(< 3 Å) are displayed as a stick model.
|
 |
|
|
|
| |
The above figures are
reprinted
from an Open Access publication published by Elsevier:
J Mol Biol
(2007,
374,
1345-1358)
copyright 2007.
|
|
| |
Figures were
selected
by an automated process.
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
 |
| |
PubMed id
|
 |
Reference
|
 |
|
|
|
 |
G.C.Atkinson,
and
S.L.Baldauf
(2011).
Evolution of elongation factor g and the origins of mitochondrial and chloroplast forms.
|
| |
Mol Biol Evol,
28,
1281-1292.
|
 |
|
|
|
|
 |
J.Dworkin,
and
I.M.Shah
(2010).
Exit from dormancy in microbial organisms.
|
| |
Nat Rev Microbiol,
8,
890-896.
|
 |
|
|
|
|
 |
A.Savelsbergh,
M.V.Rodnina,
and
W.Wintermeyer
(2009).
Distinct functions of elongation factor G in ribosome recycling and translocation.
|
| |
RNA,
15,
772-780.
|
 |
|
|
|
|
 |
M.Tsuboi,
H.Morita,
Y.Nozaki,
K.Akama,
T.Ueda,
K.Ito,
K.H.Nierhaus,
and
N.Takeuchi
(2009).
EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis.
|
| |
Mol Cell,
35,
502-510.
|
 |
|
|
|
|
 |
M.Y.Pavlov,
A.Antoun,
M.Lovmar,
and
M.Ehrenberg
(2008).
Complementary roles of initiation factor 1 and ribosome recycling factor in 70S ribosome splitting.
|
| |
EMBO J,
27,
1706-1717.
|
 |
|
 |
 |
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
|
');
}
}
| |