1kog: Difference between revisions

Revision as of 10:39, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1kog.png

Template:STRUCTURE 1kog

Crystal structure of E. coli threonyl-tRNA synthetase interacting with the essential domain of its mRNA operatorCrystal structure of E. coli threonyl-tRNA synthetase interacting with the essential domain of its mRNA operator

Template:ABSTRACT PUBMED 11953757

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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===
-==Overview==
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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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11953757}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11953757}}
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