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65 a.a.*
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68 a.a.*
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58 a.a.*
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* Residue conservation analysis
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* C-alpha coords only
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PDB id:
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Ribosome
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Title:
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Coordinates of the n-terminal domain of ribosomal protein l11,c- terminal domain of ribosomal protein l7/l12 and a portion of the g' domain of elongation factor g, as fitted into cryo-em map of an escherichia coli 70s Ef-g Gdp Fusidic acid complex
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Structure:
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50s ribosomal protein l11. Chain: a. Fragment: n-terminal domain. 50s ribosomal protein l7/l12. Chain: b. Fragment: c-terminal domain. Synonym: l8. Elongation factor g. Chain: c.
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Source:
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Thermotoga maritima. Organism_taxid: 2336. Escherichia coli. Organism_taxid: 562. Thermus thermophilus. Organism_taxid: 274
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Biol. unit:
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Trimer (from
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Authors:
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P.P.Datta,M.R.Sharma,L.Qi,J.Frank,R.K.Agrawal
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Key ref:
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P.P.Datta
et al.
(2005).
Interaction of the G' domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM.
Mol Cell,
20,
723-731.
PubMed id:
DOI:
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Date:
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19-Oct-05
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Release date:
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20-Dec-05
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Headers
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References
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P29395
(RL11_THEMA) -
Large ribosomal subunit protein uL11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
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Seq: Struc:
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141 a.a.
65 a.a.
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Enzyme class:
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Chains A, B, C:
E.C.?
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DOI no:
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Mol Cell
20:723-731
(2005)
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PubMed id:
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Interaction of the G' domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM.
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P.P.Datta,
M.R.Sharma,
L.Qi,
J.Frank,
R.K.Agrawal.
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ABSTRACT
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During tRNA translocation on the ribosome, an arc-like connection (ALC) is
formed between the G' domain of elongation factor G (EF-G) and the L7/L12-stalk
base of the large ribosomal subunit in the GDP state. To delineate the boundary
of EF-G within the ALC, we tagged an amino acid residue near the tip of the G'
domain of EF-G with undecagold, which was then visualized with three-dimensional
cryo-electron microscopy (cryo-EM). Two distinct positions for the undecagold,
observed in the GTP-state and GDP-state cryo-EM maps of the ribosome bound EF-G,
allowed us to determine the movement of the labeled amino acid. Molecular
analyses of the cryo-EM maps show: (1) that three structural components, the
N-terminal domain of ribosomal protein L11, the C-terminal domain of ribosomal
protein L7/L12, and the G' domain of EF-G, participate in formation of the ALC;
and (2) that both EF-G and the ribosomal protein L7/L12 undergo large
conformational changes to form the ALC.
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Selected figure(s)
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Figure 2.
Figure 2. Localization of Amino Acid 209C in EF-G
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Figure 3.
Figure 3. Participation of EF-G in ALC Formation
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2005,
20,
723-731)
copyright 2005.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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L.Wang,
F.Yang,
D.Zhang,
Z.Chen,
R.M.Xu,
K.H.Nierhaus,
W.Gong,
and
Y.Qin
(2012).
A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases.
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Nat Struct Mol Biol,
19,
403-410.
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K.Mikulík,
J.Bobek,
A.Ziková,
M.Smětáková,
and
S.Bezoušková
(2011).
Phosphorylation of ribosomal proteins influences subunit association and translation of poly (U) in Streptomyces coelicolor.
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Mol Biosyst,
7,
817-823.
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M.J.Han,
H.Cimen,
J.L.Miller-Lee,
H.Koc,
and
E.C.Koc
(2011).
Purification of human mitochondrial ribosomal L7/L12 stalk proteins and reconstitution of functional hybrid ribosomes in Escherichia coli.
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Protein Expr Purif,
78,
48-54.
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N.Clementi,
A.Chirkova,
B.Puffer,
R.Micura,
and
N.Polacek
(2010).
Atomic mutagenesis reveals A2660 of 23S ribosomal RNA as key to EF-G GTPase activation.
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Nat Chem Biol,
6,
344-351.
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D.J.Taylor,
B.Devkota,
A.D.Huang,
M.Topf,
E.Narayanan,
A.Sali,
S.C.Harvey,
and
J.Frank
(2009).
Comprehensive molecular structure of the eukaryotic ribosome.
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Structure,
17,
1591-1604.
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PDB codes:
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G.Y.Soung,
J.L.Miller,
H.Koc,
and
E.C.Koc
(2009).
Comprehensive analysis of phosphorylated proteins of Escherichia coli ribosomes.
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J Proteome Res,
8,
3390-3402.
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J.L.Miller,
H.Cimen,
H.Koc,
and
E.C.Koc
(2009).
Phosphorylated proteins of the mammalian mitochondrial ribosome: implications in protein synthesis.
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J Proteome Res,
8,
4789-4798.
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P.H.Too,
M.K.Ma,
A.N.Mak,
Y.T.Wong,
C.K.Tung,
G.Zhu,
S.W.Au,
K.B.Wong,
and
P.C.Shaw
(2009).
The C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosome.
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Nucleic Acids Res,
37,
602-610.
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PDB codes:
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T.Miyoshi,
T.Nomura,
and
T.Uchiumi
(2009).
Engineering and Characterization of the Ribosomal L10{middle dot}L12 Stalk Complex: A STRUCTURAL ELEMENT RESPONSIBLE FOR HIGH TURNOVER OF THE ELONGATION FACTOR G-DEPENDENT GTPase.
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J Biol Chem,
284,
85-92.
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Y.G.Gao,
M.Selmer,
C.M.Dunham,
A.Weixlbaumer,
A.C.Kelley,
and
V.Ramakrishnan
(2009).
The structure of the ribosome with elongation factor G trapped in the posttranslocational state.
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Science,
326,
694-699.
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PDB codes:
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J.M.Harms,
D.N.Wilson,
F.Schluenzen,
S.R.Connell,
T.Stachelhaus,
Z.Zaborowska,
C.M.Spahn,
and
P.Fucini
(2008).
Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin.
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Mol Cell,
30,
26-38.
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PDB codes:
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M.Hu,
L.Qian,
R.P.Briñas,
E.S.Lymar,
L.Kuznetsova,
and
J.F.Hainfeld
(2008).
Gold nanoparticle-protein arrays improve resolution for cryo-electron microscopy.
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J Struct Biol,
161,
83-91.
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O.Kurkcuoglu,
P.Doruker,
T.Z.Sen,
A.Kloczkowski,
and
R.L.Jernigan
(2008).
The ribosome structure controls and directs mRNA entry, translocation and exit dynamics.
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Phys Biol,
5,
046005.
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P.Chandramouli,
M.Topf,
J.F.Ménétret,
N.Eswar,
J.J.Cannone,
R.R.Gutell,
A.Sali,
and
C.W.Akey
(2008).
Structure of the mammalian 80S ribosome at 8.7 A resolution.
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Structure,
16,
535-548.
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PDB codes:
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R.N.Evans,
G.Blaha,
S.Bailey,
and
T.A.Steitz
(2008).
The structure of LepA, the ribosomal back translocase.
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Proc Natl Acad Sci U S A,
105,
4673-4678.
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PDB code:
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A.García-Marcos,
A.Morreale,
E.Guarinos,
E.Briones,
M.Remacha,
A.R.Ortiz,
and
J.P.Ballesta
(2007).
In vivo assembling of bacterial ribosomal protein L11 into yeast ribosomes makes the particles sensitive to the prokaryotic specific antibiotic thiostrepton.
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Nucleic Acids Res,
35,
7109-7117.
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C.Barat,
P.P.Datta,
V.S.Raj,
M.R.Sharma,
H.Kaji,
A.Kaji,
and
R.K.Agrawal
(2007).
Progression of the ribosome recycling factor through the ribosome dissociates the two ribosomal subunits.
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Mol Cell,
27,
250-261.
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D.Lee,
J.D.Walsh,
P.Yu,
M.A.Markus,
T.Choli-Papadopoulou,
C.D.Schwieters,
S.Krueger,
D.E.Draper,
and
Y.X.Wang
(2007).
The structure of free L11 and functional dynamics of L11 in free, L11-rRNA(58 nt) binary and L11-rRNA(58 nt)-thiostrepton ternary complexes.
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J Mol Biol,
367,
1007-1022.
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PDB codes:
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D.Pan,
S.V.Kirillov,
and
B.S.Cooperman
(2007).
Kinetically competent intermediates in the translocation step of protein synthesis.
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Mol Cell,
25,
519-529.
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N.Gao,
A.V.Zavialov,
M.Ehrenberg,
and
J.Frank
(2007).
Specific interaction between EF-G and RRF and its implication for GTP-dependent ribosome splitting into subunits.
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J Mol Biol,
374,
1345-1358.
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PDB code:
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R.Nechifor,
M.Murataliev,
and
K.S.Wilson
(2007).
Functional Interactions between the G' Subdomain of Bacterial Translation Factor EF-G and Ribosomal Protein L7/L12.
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J Biol Chem,
282,
36998-37005.
|
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S.R.Connell,
C.Takemoto,
D.N.Wilson,
H.Wang,
K.Murayama,
T.Terada,
M.Shirouzu,
M.Rost,
M.Schüler,
J.Giesebrecht,
M.Dabrowski,
T.Mielke,
P.Fucini,
S.Yokoyama,
and
C.M.Spahn
(2007).
Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors.
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Mol Cell,
25,
751-764.
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PDB code:
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V.Berk,
and
J.H.Cate
(2007).
Insights into protein biosynthesis from structures of bacterial ribosomes.
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Curr Opin Struct Biol,
17,
302-309.
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Y.Maki,
T.Hashimoto,
M.Zhou,
T.Naganuma,
J.Ohta,
T.Nomura,
C.V.Robinson,
and
T.Uchiumi
(2007).
Three binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism.
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J Biol Chem,
282,
32827-32833.
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D.Qiu,
P.Parada,
A.G.Marcos,
D.Cárdenas,
M.Remacha,
and
J.P.Ballesta
(2006).
Different roles of P1 and P2 Saccharomyces cerevisiae ribosomal stalk proteins revealed by cross-linking.
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Mol Microbiol,
62,
1191-1202.
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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.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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}
}
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