CATH Domain 4o2dA01

CATH Classification

Level	CATH Code	Description
	2	Mainly Beta
	2.40	Beta Barrel
	2.40.50	OB fold (Dihydrolipoamide Acetyltransferase, E2P)
	2.40.50.140	Nucleic acid-binding proteins

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	4O2D
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Increasing the structural coverage of tuberculosis drug targets. Baugh, L., Phan, I., Begley, D.W., Clifton, M.C., Armour, B., Dranow, D.M., Taylor, B.M., Muruthi, M.M., Abendroth, J., Fairman, J.W., Fox, D., Dieterich, S.H., Staker, B.L., Gardberg, A.S., Choi, R., Hewitt, S.N., Napuli, A.J., Myers, J., Barrett, L.K., Zhang, Y., Ferrell, M., Mundt, E., Thompkins, K., Tran, N., Lyons-Abbott, S., Abramov, A., Sekar, A., Serbzhinskiy, D., Lorimer, D., Buchko, G.W., Stacy, R., Stewart, L.J., Edwards, T.E., Van Voorhis, W.C., Myler, P.J. Tuberculosis (Edinb)