CATH Classification

Domain Context

CATH Clusters

Superfamily Nucleic acid-binding proteins
Functional Family

Enzyme Information

6.1.1.23
Aspartate--tRNA(Asn) ligase.
based on mapping to UniProt A0QWN3
ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx).
-!- When this enzyme acts on tRNA(Asp), it catalyzes the same reaction as EC 6.1.1.12. -!- It has, however, diminished discrimination, so that it can also form aspartyl-tRNA(Asn). -!- This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon. -!- This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNA(Asp) (GUC anticodon) and tRNA(Asn) (GUU anticodon). -!- The aspartate-tRNA(Asn) is not used in protein synthesis until it is converted by EC 6.3.5.6 into asparaginyl-tRNA(Asn).

UniProtKB Entries (1)

A0QWN3
SYDND_MYCS2
Mycolicibacterium smegmatis MC2 155
Aspartate--tRNA(Asp/Asn) ligase

PDB Structure

PDB 4RMF
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Biochemical and Structural Characterization of Mycobacterial Aspartyl-tRNA Synthetase AspS, a Promising TB Drug Target.
Gurcha, S.S., Usha, V., Cox, J.A., Futterer, K., Abrahams, K.A., Bhatt, A., Alderwick, L.J., Reynolds, R.C., Loman, N.J., Nataraj, V., Alemparte, C., Barros, D., Lloyd, A.J., Ballell, L., Hobrath, J.V., Besra, G.S.
Plos One