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PDBsum entry 1kog
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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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Structural basis of translational control by escherichia coli threonyl tRNA synthetase.
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Authors
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A.Torres-Larios,
A.C.Dock-Bregeon,
P.Romby,
B.Rees,
R.Sankaranarayanan,
J.Caillet,
M.Springer,
C.Ehresmann,
B.Ehresmann,
D.Moras.
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Ref.
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Nat Struct Biol, 2002,
9,
343-347.
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PubMed id
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Abstract
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Escherichia coli threonyl-tRNA synthetase (ThrRS) represses the translation of
its own messenger RNA by binding to an operator located upstream of the
initiation codon. The crystal structure of the complex between the core of ThrRS
and the essential domain of the operator shows that the mRNA uses the
recognition mode of the tRNA anticodon loop to initiate binding. The final
positioning of the operator, upon which the control mechanism is based, relies
on a characteristic RNA motif adapted to the enzyme surface. The finding of
other thrS operators that have this conserved motif leads to a generalization of
this regulatory mechanism to a subset of Gram-negative bacteria.
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