Crystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus bound to proline sulfamoyl adenylate

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

Prolyl-tRNA synthetase; Proline--tRNA ligase; ProRS

MGSSHHHHHHSSGLVPRGSHMQKPIKKDPNRYHGEKMTEFSEWFHNILEEAEIIDQRYPVKGMHVWMPHGFMIRKNTLKI
LRRILDRDHEEVLFPLLVPEDELAKEAIHVKGFEDEVYWVTHGGLSKLQRKLALRPTSETVMYPMFALWVRSHTDLPMRF
YQVVNTFRYETKHTRPLIRVREITTFKEAHTIHATASEAEEQVERAVEIYKEFFNSLGIPYLITRRPPWDKFPGSEYTVA
FDTLMPDGKTLQIGTVHNLGQTFARTFEIKFETPEGDHEYVHQTCYGLSDRVIASVIAIHGDESGLCLPPDVAAHQVVIV
PIIFKKAAEEVMEACRELRSRLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGEKVTAD
LQGIEETLRELMKDILENLRTRAWERMESEIREAETLEEASRIVDEKRGIISFMWCGEEECGMDVEEKVRVDILGIQEEG
SGTCINCGREAPYRAYLARTY

Strain supplemented with additional plasmid encoding rare tRNAs

Tris, Beta-Mercaptoethanol, MgCl2,NaCl, Proline sulfamoyl adenylate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Methanocaldococcus janaschii Proline tRNA Synthetase

The biological assembly is a dimer constructed by a twofold rotation.

Protein-Aminoacyladenylate Complex Class-II tRNA synthetase, LIGASE

MQKPIKKDPNRYHGEKMTEFSEWFHNILEEAEIIDQRYPVKGMHVWMPHGFMIRKNTLKILRRILDRDHEEVLFPLLVPE
DELAKEAIHVKGFEDEVYWVTHGGLSKLQRKLALRPTSETVMYPMFALWVRSHTDLPMRFYQVVNTFRYETKHTRPLIRV
REITTFKEAHTIHATASEAEEQVERAVEIYKEFFNSLGIPYLITRRPPWDKFPGSEYTVAFDTLMPDGKTLQIGTVHNLG
QTFARTFEIKFETPEGDHEYVHQTCYGLSDRVIASVIAIHGDESGLCLPPDVAAHQVVIVPIIFKKAAEEVMEACRELRS
RLEAAGFRVHLDDRDIRAGRKYYEWEMRGVPLRVEIGPRDLEKGAAVISRRDTGEKVTADLQGIEETLRELMKDILENLR
TRAWERMESEIREAETLEEASRIVDEKRGIISFMWCGEEECGMDVEEKVRVDILGIQEEGSGTCINCGREAPTGLTLPEH
IS