9SLZ

Structure of Thermus thermophilus lysyl-tRNA synthetase complexed with wild-type E.coli tRNALys(mnm5s2UUU) and sulphamoyl-analogue of lysyl-adenylate

Summary for 9SLZ

• Entry DOI: 10.2210/pdb9slz/pdb
• Descriptor: Lysine--tRNA ligase, Wild-type E. coli tRNALys, SULFATE ION, ... (4 entities in total)
• Functional Keywords: amino-acyl-trna synthetase, trna, aminoacyl-adenylate, rna binding protein
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 2
• Total formula weight: 83137.20

Authors

Cusack, S.,Yaremchuk, A.,Tukalo, M. (deposition date: 2025-09-05, release date: 2025-09-17)

Primary citation

Cusack, S.,Yaremchuk, A.,Tukalo, M.
The crystal structures of T. thermophilus lysyl-tRNA synthetase complexed with E. coli tRNA(Lys) and a T. thermophilus tRNA(Lys) transcript: anticodon recognition and conformational changes upon binding of a lysyl-adenylate analogue.
EMBO J, 15:6321-6334, 1996

PubMed Abstract: The crystal structures of Thermus thermophilus lysyl-tRNA synthetase, a class IIb aminoacyl-tRNA synthetase, complexed with Escherchia coli tRNA(Lys)(mnm5 s2UUU) at 2.75 A resolution and with a T. thermophilus tRNA(Lys)(CUU) transcript at 2.9 A resolution are described. In both complexes only the tRNA anticodon stem-loop is well ordered. The mode of binding of the anticodon stem-loop to the N-terminal beta-barrel domain is similar to that previously found for the homologous class IIb aspartyl-tRNA synthetase-tRNA(Asp) complex except in the region of the wobble base 34 where either mnm5 s2U or C can be accommodated. The specific recognition of the other anticodon bases, U-35 and U-36, which are both major identity elements in the lysine system, is also described. Additional crystallographic data on a ternary complex with a lysyl-adenylate analogue show that binding of the intermediate induces significant conformational changes in the vicinity of the active site of the enzyme.

PubMed: 8947055

Experimental method

X-RAY DIFFRACTION (3.8 Å)