1kog: Difference between revisions
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'''Crystal structure of E. coli threonyl-tRNA synthetase interacting with the essential domain of its mRNA operator''' | '''Crystal structure of E. coli threonyl-tRNA synthetase interacting with the essential domain of its mRNA operator''' | ||
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[[Category: Springer, M.]] | [[Category: Springer, M.]] | ||
[[Category: Torres-Larrios, A.]] | [[Category: Torres-Larrios, A.]] | ||
[[Category: | [[Category: Protein-rna complex]] | ||
[[Category: | [[Category: Rna base triple]] | ||
[[Category: | [[Category: Rna double helix]] | ||
[[Category: | [[Category: Rna stem-loop]] | ||
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Revision as of 22:59, 2 May 2008
Crystal structure of E. coli threonyl-tRNA synthetase interacting with the essential domain of its mRNA operator
OverviewOverview
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.
About this StructureAbout this Structure
1KOG is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of translational control by Escherichia coli threonyl tRNA synthetase., Torres-Larios A, Dock-Bregeon AC, Romby P, Rees B, Sankaranarayanan R, Caillet J, Springer M, Ehresmann C, Ehresmann B, Moras D, Nat Struct Biol. 2002 May;9(5):343-7. PMID:11953757 Page seeded by OCA on Fri May 2 22:59:00 2008