CATH Domain 1vlrB02

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.30	2-Layer Sandwich
	3.30.2240	mRNA decapping enzyme DcpS N-terminal fold
	3.30.2240.10	mRNA decapping enzyme DcpS N-terminal domain

Domain Context

CATH Clusters

Superfamily	mRNA decapping enzyme DcpS N-terminal domain
Functional Family

Enzyme Information

3.6.1.59

5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase.

based on mapping to UniProt Q9DAR7

A 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] + H(2)O = N(7)- methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA].

-!- The enzyme removes (decaps) the N(7)-methylguanosine 5-phosphate cap from an mRNA degraded to a maximal length of 10 nucleotides. -!- Decapping is an important process in the control of eukaryotic mRNA degradation. -!- The enzyme functions to clear the cell of cap structure following decay of the RNA body. -!- The nematode enzyme can also decap triply methylated substrates, 5'-(N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-[mRNA]. -!- Formerly EC 3.6.1.30.

UniProtKB Entries (1)

Q9DAR7

DCPS_MOUSE

Mus musculus

M7GpppX diphosphatase

PDB Structure

PDB	1VLR
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Crystal structure of an Apo mRNA decapping enzyme (DcpS) from Mouse at 1.83 A resolution. Han, G.W., Schwarzenbacher, R., McMullan, D., Abdubek, P., Ambing, E., Axelrod, H., Biorac, T., Canaves, J.M., Chiu, H.J., Dai, X., Deacon, A.M., DiDonato, M., Elsliger, M.A., Godzik, A., Grittini, C., Grzechnik, S.K., Hale, J., Hampton, E., Haugen, J., Hornsby, M., Jaroszewski, L., Klock, H.E., Koesema, E., Kreusch, A., Kuhn, P., Lesley, S.A., McPhillips, T.M., Miller, M.D., Moy, K., Nigoghossian, E., Paulsen, J., Quijano, K., Reyes, R., Spraggon, G., Stevens, R.C., van den Bedem, H., Velasquez, J., Vincent, J., White, A., Wolf, G., Xu, Q., Hodgson, K.O., Wooley, J., Wilson, I.A. Proteins

Network disruptions