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PDBsum entry 2id0
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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 basis for processivity and single-Strand specificity of rnase ii.
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Authors
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Y.Zuo,
H.A.Vincent,
J.Zhang,
Y.Wang,
M.P.Deutscher,
A.Malhotra.
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Ref.
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Mol Cell, 2006,
24,
149-156.
[DOI no: ]
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PubMed id
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Abstract
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RNase II is a member of the widely distributed RNR family of exoribonucleases,
which are highly processive 3'-->5' hydrolytic enzymes that play an important
role in mRNA decay. Here, we report the crystal structure of E. coli RNase II,
which reveals an architecture reminiscent of the RNA exosome. Three RNA-binding
domains come together to form a clamp-like assembly, which can only accommodate
single-stranded RNA. This leads into a narrow, basic channel that ends at the
putative catalytic center that is completely enclosed within the body of the
protein. The putative path for RNA agrees well with biochemical data indicating
that a 3' single strand overhang of 7-10 nt is necessary for binding and
hydrolysis by RNase II. The presence of the clamp and the narrow channel
provides an explanation for the processivity of RNase II and for why its action
is limited to single-stranded RNA.
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Figure 2.
Figure 2. RNase II Active Center
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Figure 3.
Figure 3. Proposed Mechanism for RNase II ssRNA Specificity
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2006,
24,
149-156)
copyright 2006.
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