PDBsum entry 4xwt

RNA binding protein

PDB id: 4xwt

Contents

Protein chains

543 a.a.

Ligands

GOL ×2

U5P ×2

Metals

_ZN ×4

_MN ×2

Waters ×322

PDB id:

4xwt

Name:

RNA binding protein

Title:

Crystal structure of rnase j complexed with ump

Structure:

Dr2417. Chain: a, b. Engineered: yes

Source:

Deinococcus radiodurans. Organism_taxid: 1299. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.202 R-free: 0.235

Authors:

M.Lu,H.Zhang,Q.Xu,Y.Hua,Y.Zhao

Key ref:

Y.Zhao et al. (2015). Structural insights into catalysis and dimerization enhanced exonuclease activity of RNase J. Nucleic Acids Res, 43, 5550-5559. PubMed id: 25940620 DOI: 10.1093/nar/gkv444

Date:

29-Jan-15 Release date: 16-Dec-15

Protein chains

H9CZL7  (H9CZL7_DEIRD) -  Ribonuclease J from Deinococcus radiodurans

Seq: 559 a.a.

Struc: 543 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.-.-

DOI no: 10.1093/nar/gkv444

Nucleic Acids Res 43:5550-5559 (2015)

PubMed id: 25940620

Structural insights into catalysis and dimerization enhanced exonuclease activity of RNase J.

Y.Zhao, M.Lu, H.Zhang, J.Hu, C.Zhou, Q.Xu, A.M.Ul Hussain Shah, H.Xu, L.Wang, Y.Hua.

ABSTRACT

RNase J is a conserved ribonuclease that belongs to the β-CASP family of nucleases. It possesses both endo- and exo-ribonuclease activities, which play a key role in pre-rRNA maturation and mRNA decay. Here we report high-resolution crystal structures of Deinococcus radiodurans RNase J complexed with RNA or uridine 5'-monophosphate in the presence of manganese ions. Biochemical and structural studies revealed that RNase J uses zinc ions for two-metal-ion catalysis. One residue conserved among RNase J orthologues (motif B) forms specific electrostatic interactions with the scissile phosphate of the RNA that is critical for the catalysis and product stabilization. The additional manganese ion, which is coordinated by conserved residues at the dimer interface, is critical for RNase J dimerization and exonuclease activity. The structures may also shed light on the mechanism of RNase J exo- and endonucleolytic activity switch.