4RO1

An 3'-5'-exoribonuclease that specifically recognizes RNAs.

Summary for 4RO1

• Entry DOI: 10.2210/pdb4ro1/pdb
• Descriptor: DIS3-like exonuclease 2 (1 entity in total)
• Functional Keywords: ob-folds and rnb, rna digestion, hydrolase
• Biological source: Schizosaccharomyces pombe (Fission yeast)
• Cellular location: Cytoplasm : O14040
• Total number of polymer chains: 2
• Total formula weight: 174131.22

Authors

Lv, H.,Zhu, Y.,Teng, M. (deposition date: 2014-10-27, release date: 2015-06-10, Last modification date: 2024-02-28)

Primary citation

Lv, H.,Zhu, Y.,Qiu, Y.,Niu, L.,Teng, M.,Li, X.
Structural analysis of Dis3l2, an exosome-independent exonuclease from Schizosaccharomyces pombe.
Acta Crystallogr.,Sect.D, 71:1284-1294, 2015

PubMed Abstract: After deadenylation and decapping, cytoplasmic mRNA can be digested in two opposite directions: in the 5'-3' direction by Xrn1 or in the 3'-5' direction by the exosome complex. Recently, a novel 3'-5' RNA-decay pathway involving Dis3l2 has been described that differs from degradation by Xrn1 and the exosome. The product of the Schizosaccharomyces pombe gene SPAC2C4.07c was identified as a homologue of human Dis3l2. In this work, the 2.8 Å resolution X-ray crystal structure of S. pombe Dis3l2 (SpDis3l2) is reported, the conformation of which is obviously different from that in the homologous mouse Dis3l2-RNA complex. Fluorescence polarization assay experiments showed that RNB and S1 are the primary RNA-binding domains and that the CSDs (CSD1 and CSD2) play an indispensable role in the RNA-binding process of SpDis3l2. Taking the structure comparison and mutagenic experiments together, it can be inferred that the RNA-recognition pattern of SpDis3l2 resembles that of its mouse homologue rather than that of the Escherichia coli RNase II-RNA complex. Furthermore, a drastic conformation change could occur following the binding of the RNA substrate to SpDis3l2.

PubMed: 26057668
DOI: 10.1107/S1399004715005805

Experimental method

X-RAY DIFFRACTION (2.803 Å)