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2.7.1.164: O-phosphoseryl-tRNASec kinase

This is an abbreviated version!
For detailed information about O-phosphoseryl-tRNASec kinase, go to the full flat file.

Word Map on EC 2.7.1.164

Reaction

ATP
+
L-seryl-tRNASec
=
ADP
 +
O-phospho-L-seryl-tRNASec

Synonyms

O-phosphoseryl-tRNA kinase, O-phosphoseryl-tRNA(Sec) kinase, O-phosphoseryl-tRNASec kinase, phosphoseryl-tRNASec kinase, phosphoseryl-tRNA[Ser]Sec kinase, PSTK, Tb10.6k15.1110, TbPSTK

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.164 O-phosphoseryl-tRNASec kinase

Crystallization

Crystallization on EC 2.7.1.164 - O-phosphoseryl-tRNASec kinase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with an anticodon-stem/loop truncated tRNASec, to 2.4 A resolution. Truncated tRNASec is bound between the enzyme's C-terminal domain CTD and N-terminal kinase domain NTD that are connected by a flexible 11 amino acid linker. Upon tRNASec recognition, the CTD undergoes a 62-A movement to allow proper binding of the 7-bp D-stem. This large reorganization of the quaternary structure likely provides a means by which the unique tRNASec species can be accurately recognized with high affinity by the translation machinery
in complex with Methanopyrus tRNASec and with 5'-adenylyl imidodiphosphate, to 2.5-2.9 A resolution. The enzyme consists of two independent linker-connected domains, the N-terminal catalytic domain NTD and the C-terminal domain CTD. The D-arm-CTD binding occurs independently of and much more strongly than the acceptor-arm-NTD binding. The enzyme thereby distinguishes the characteristic D arm with the maximal stem and the minimal loop of tRNASec from the canonical D arm of tRNASer, without interacting with the anticodon
sitting drop vapor diffusion method at 20°C, the structures of MjPSTK complexed with ADP and AMPPNP revealed that this enzyme belongs to the P-loop kinase class, and that the kinase domain is closely related to gluconate kinase and adenylate kinase. ATP is bound by the P-loop domain (residues 11-18). Formed by antiparallel dimerization of two O-phosphoseryl-tRNASec kinase monomers, the enzyme structure shows a deep groove with positive electrostatic potential. Located in this groove is the active site of the enzyme, which biochemical and genetic data suggest is composed of Asp-41, Arg-44, Glu-55, Tyr-82, Tyr-83, Met-86, and Met-132