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PDBsum entry 3j5s
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Ribosome/translation
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PDB id
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3j5s
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Contents |
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554 a.a.
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234 a.a.
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178 a.a.
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50 a.a.
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151 a.a.
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PDB id:
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Ribosome/translation
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Title:
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Etta binds to ribosome exit site and regulates translation by restricting ribosome and tRNA dynamics
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Structure:
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16s ribosomal RNA. Chain: b. Fragment: see remark 999. 23s ribosomal RNA. Chain: a. Fragment: see remark 999. P-site tRNA fmet. Chain: e. Energy-dependent translational throttle a (etta).
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Source:
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Escherichia coli. Organism_taxid: 562. Strain: mre600. Organism_taxid: 511145. Strain: k12 substr. Mg1655. Gene: yjjk. Expressed in: escherichia coli. Expression_system_taxid: 511145. Strain: mre600
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Authors:
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Y.Hashem
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Key ref:
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B.Chen
et al.
(2014).
EttA regulates translation by binding the ribosomal E site and restricting ribosome-tRNA dynamics.
Nat Struct Biol,
21,
152-159.
PubMed id:
DOI:
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Date:
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15-Nov-13
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Release date:
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08-Jan-14
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PROCHECK
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Headers
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References
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P0A9W3
(ETTA_ECOLI) -
Energy-dependent translational throttle protein EttA from Escherichia coli (strain K12)
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Seq: Struc:
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555 a.a.
554 a.a.
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P0A7L0
(RL1_ECOLI) -
Large ribosomal subunit protein uL1 from Escherichia coli (strain K12)
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Seq: Struc:
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234 a.a.
234 a.a.
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P62399
(RL5_ECOLI) -
Large ribosomal subunit protein uL5 from Escherichia coli (strain K12)
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Seq: Struc:
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179 a.a.
178 a.a.
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Enzyme class 2:
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Chain D:
E.C.3.6.1.-
- ?????
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Enzyme class 3:
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Chains F, G, H, I:
E.C.?
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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.
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DOI no:
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Nat Struct Biol
21:152-159
(2014)
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PubMed id:
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EttA regulates translation by binding the ribosomal E site and restricting ribosome-tRNA dynamics.
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B.Chen,
G.Boël,
Y.Hashem,
W.Ning,
J.Fei,
C.Wang,
R.L.Gonzalez,
J.F.Hunt,
J.Frank.
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ABSTRACT
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Cells express many ribosome-interacting factors whose functions and molecular
mechanisms remain unknown. Here, we elucidate the mechanism of a newly
characterized regulatory translation factor, energy-dependent translational
throttle A (EttA), which is an Escherichia coli representative of the
ATP-binding cassette F (ABC-F) protein family. Using cryo-EM, we demonstrate
that the ATP-bound form of EttA binds to the ribosomal tRNA-exit site, where it
forms bridging interactions between the ribosomal L1 stalk and the tRNA bound in
the peptidyl-tRNA-binding site. Using single-molecule fluorescence resonance
energy transfer, we show that the ATP-bound form of EttA restricts ribosome and
tRNA dynamics required for protein synthesis. This work represents the first
example, to our knowledge, in which the detailed molecular mechanism of any
ABC-F family protein has been determined and establishes a framework for
elucidating the mechanisms of other regulatory translation factors.
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');
}
}
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