1KOG

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

Summary for 1KOG

• Entry DOI: 10.2210/pdb1kog/pdb
• Related: 1EVL 1QF6
• Descriptor: Threonyl-tRNA synthetase mRNA, Threonyl-tRNA synthetase, ZINC ION, ... (5 entities in total)
• Functional Keywords: protein-rna complex, rna stem-loop, rna double helix, rna base triples, ligase-rna complex, ligase/rna
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A8M3
• Total number of polymer chains: 16
• Total formula weight: 472575.94

Authors

Torres-Larrios, A.,Dock-Bregeon, A.C.,Romby, P.,Rees, B.,Sankaranarayanan, R.,Caillet, J.,Springer, M.,Ehresmann, C.,Ehresmann, B.,Moras, D. (deposition date: 2001-12-20, release date: 2002-04-26, Last modification date: 2023-08-16)

Primary citation

Torres-Larios, A.,Dock-Bregeon, A.C.,Romby, P.,Rees, B.,Sankaranarayanan, R.,Caillet, J.,Springer, M.,Ehresmann, C.,Ehresmann, B.,Moras, D.
Structural basis of translational control by Escherichia coli threonyl tRNA synthetase.
Nat.Struct.Biol., 9:343-347, 2002

PubMed Abstract: 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.

PubMed: 11953757

Experimental method

X-RAY DIFFRACTION (3.5 Å)