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PDBsum entry 5y9p
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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 a novel functional dimer of staphylococcus aureus rnase hii.
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Authors
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T.Hang,
X.Zhang,
M.Wu,
C.Wang,
S.Ling,
L.Xu,
Q.Gong,
C.Tian,
X.Zhang,
J.Zang.
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Ref.
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Biochem Biophys Res Commun, 2018,
503,
1207-1213.
[DOI no: ]
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PubMed id
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Abstract
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RNase HII exists ubiquitously in organisms and functions as a monomer in
prokaryotes. We determined the crystal structure of Staphylococcus aureus RNase
HII (Sa-RNase HII), which displays a novel dimer conformation, with the active
site of each monomer covered by the other one. Both small-angle X-ray scattering
and gel-filtration analysis confirmed that Sa-RNase HII exists as a homodimer in
solution. Enzymatic analysis revealed that the "self-inhibited"
dimeric form is catalytically active. Furthermore, continuous-wave electron
paramagnetic resonance experiments clarified that the Sa-RNase HII dimer
undergoes a large conformational change upon substrate binding, but remains a
dimer to catalyze the reaction. Our structural and biochemical studies
identified a novel functional dimer of Sa-RNase HII with distinct regulation
mechanism for its catalytic activity.
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