| Title | Crystal structure of Glycyl-tRNA synthetase alpha chain (TM0216) from Thermotoga maritima at 1.95 A resolution. To be published | | Site | JCSG | | PDB Id | | Target Id | 282096 | | Molecular Characteristics | | Source | Thermotoga maritima msb8 | | Alias Ids | TPS1193,TM0216 | Molecular Weight | 33538.30 Da. | | Residues | 286 | Isoelectric Point | 4.99 | | Sequence | mylqdvimklndfwaskgclleqpydmevgagtfhpatffgslrkgpwkvayvqpsrrptdgrygenpn rlqryfqyqviikpspensqelylesleylginlkehdirfvednwesptlgawgvgwevwldgmeitq ftyfqqiggislkdipleitygleriamylqgvdnvyevqwnenvkygdvflenerefsvfnfeeanvg llfrhfdeyekefyrlveknlylpaydyilkcshtfnlldargaisvsqrqtyvkriqamarkaarvfl evqanenspa | | | BLAST FFAS | | Structure Determination | | Method | XRAY | Chains | 2 | | Resolution (Å) | 1.95 | Rfree | 0.254 | | Matthews' coefficent | 2.27 | Rfactor | 0.197 | | Waters | 255 | Solvent Content | 45.49 |
| Pathway | | Reactions found in Metabolic Reconstruction for TM0216 | Name: Glycyl-tRNA synthetase
Other genes that carryout this rxn:TM0217
Metabolic Subsystem: tRNA Metabolism
Reaction: :
atp
Name:ATP
Formula:C10H12N5O13P3
KEGG:
C00002
+
gly
Name:Glycine
Formula:C2H5NO2
KEGG:
C00037
+
trnagly
Name:tRNA(Gly)
Formula:R
KEGG:
C01642
-->
amp
Name:AMP
Formula:C10H12N5O7P
KEGG:
C00020
+
glytrna
Name:Glycyl-tRNA(Gly)
Formula:C2H4NOR
KEGG:
C02412
+
ppi
Name:Diphosphate
Formula:HO7P2
KEGG:
C00013
Classification: EC:6.1.1.14
|
| Ligand Information | | Ligands | | | Metals | | | |
Protein Summary
The TM0216 from Thermotoga maritima codes for glycyl-tRNA synthetase alpha chain. The enzyme belongs to a family of class II tRNA synthetases PF02091. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II COG0752. These proteins differ widely in size and oligomeric state, and have limited sequence homology [Ref]. However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred.
Ligand Summary
References
