EC Number   |
Subunits |
Reference |
|---|
   6.1.1.26 | ? |
x * 51000, full-length enzyme, SDS-PAGE, x * 33000, recombinant N-terminally truncated enzyme form PylRS(c270), SDS-PAGE |
671091 |
| 6.1.1.26 | dimer |
- |
693638 |
| 6.1.1.26 | dimer |
crystallization data |
705880 |
| 6.1.1.26 | dimer |
molecular dynamics simulations of the structures of PylRS and its complexes with tRNAPyl and activated pyrrolysine, overview. Identification of key residues and interactions leading to shortest paths of communication in the structure networks of DhPylRS. Dmeric hPylRS in different states of ligation: Sys1 as native DhPylRS, Sys2 as DhPylRS-Pyl-AMP, and Sys3 as DhPylRS-Pyl-AMP-tRNA, detailed overview |
714264 |
| 6.1.1.26 | dimer |
the PylRS catalytic core resembles that of other synthetases from the Class II AARS family. It has a typical beta-sheet core surrounded by several helices, forming a Rossmann fold for the binding of ATP. Like most other class II aminoacyl-tRNA synthetases, PylRS also forms an obligate dimer. Each subunit has an active site |
-, 744388 |
| 6.1.1.26 | homodimer |
architecture typical of the catalytic domains of class II aminoacyl-tRNA synthetases (aaRSs) |
690746 |
| 6.1.1.26 | homodimer |
x-ray crystallography |
-, 726549 |
| 6.1.1.26 | More |
PylRS is mainly composed of two domains: the N-terminal RNA-binding domain and the C-terminal aaRS catalytic domain |
671091 |
| 6.1.1.26 | More |
the PylRS sequence can be subdivided into three regions: the highly conserved class II aaRS catalytic core domain at the carboxy-terminal, the unique amino-terminal domain, and a highly variable region linking these two domains |
673691 |
| 6.1.1.26 | More |
the PylRS sequence can be subdivided into three regions: the highly conserved class II aaRS catalytic core domain at the carboxy-terminal, the unique amino-terminal domain, and a highly variable region linking these two domains, residues from the PylRS amino-terminal domain affect activity in vivo |
673691 |
