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PDBsum entry 4xwt
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RNA binding protein
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PDB id
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4xwt
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References listed in PDB file
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Key reference
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Title
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Structural insights into catalysis and dimerization enhanced exonuclease activity of rnase j.
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Authors
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Y.Zhao,
M.Lu,
H.Zhang,
J.Hu,
C.Zhou,
Q.Xu,
A.M.Ul hussain shah,
H.Xu,
L.Wang,
Y.Hua.
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Ref.
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Nucleic Acids Res, 2015,
43,
5550-5559.
[DOI no: ]
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PubMed id
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Abstract
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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.
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