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PDBsum entry 5aoy
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References listed in PDB file
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Key reference
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Title
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Crystal structure and md simulation of mouse endov reveal wedge motif plasticity in this inosine-Specific endonuclease.
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Authors
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M.S.Nawaz,
E.S.Vik,
M.E.Ronander,
A.M.Solvoll,
P.Blicher,
M.Bjørås,
I.Alseth,
B.Dalhus.
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Ref.
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Sci Rep, 2016,
6,
24979.
[DOI no: ]
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PubMed id
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Abstract
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Endonuclease V (EndoV) is an enzyme with specificity for deaminated adenosine
(inosine) in nucleic acids. EndoV from Escherichia coli (EcEndoV) acts both on
inosines in DNA and RNA, whereas the human homolog cleaves only at inosines in
RNA. Inosines in DNA are mutagenic and the role of EndoV in DNA repair is well
established. In contrast, the biological function of EndoV in RNA processing is
largely unexplored. Here we have characterized a second mammalian EndoV homolog,
mouse EndoV (mEndoV), and show that mEndoV shares the same RNA selectivity as
human EndoV (hEndoV). Mouse EndoV cleaves the same inosine-containing substrates
as hEndoV, but with reduced efficiencies. The crystal structure of mEndoV
reveals a conformation different from the hEndoV and prokaryotic EndoV
structures, particularly for the conserved tyrosine in the wedge motif,
suggesting that this strand separating element has some flexibility. Molecular
dynamics simulations of mouse and human EndoV reveal alternative conformations
for the invariant tyrosine. The configuration of the active site, on the other
hand, is very similar between the prokaryotic and mammalian versions of EndoV.
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