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- W2080304317 abstract "LC11-RNase H1 is a Sulfolobus tokodaii RNase H1 (Sto-RNase H1) homologue isolated by metagenomic approach. In this study, the crystal structure of LC11-RNase H1 in complex with an RNA/DNA substrate was determined. Unlike Bacillus halodurans RNase H1 without hybrid binding domain (HBD) (Bh-RNase HC) and human RNase H1 without HBD (Hs-RNase HC), LC11-RNase H1 interacts with four non-consecutive 2′-OH groups of the RNA strand. The lack of interactions with four consecutive 2′-OH groups leads to a dramatic decrease in the ability of LC11-RNase H1 to cleave the DNA–RNA–DNA/DNA substrate containing four ribonucleotides as compared to those to cleave the substrates containing five and six ribonucleotides. The interaction of LC11-RNase H1 with the DNA strand is also different from those of Bh-RNase HC and Hs-RNase HC. Beside the common phosphate-binding pocket, LC11-RNase H1 has a unique DNA-binding channel. Furthermore, the active-site residues of LC11-RNase H1 are located farther away from the scissile phosphate group than those of Bh-RNase HC and Hs-RNase HC. Modeling of Sto-RNase H1 in complex with the 14 bp RNA/DNA substrate, together with the structure-based mutational analyses, suggest that the ability of Sto-RNase H1 to cleave double-stranded RNA is dependent on the local conformation of the basic residues located at the DNA binding site." @default.
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- W2080304317 date "2013-05-01" @default.
- W2080304317 modified "2023-10-14" @default.
- W2080304317 title "Crystal structure of metagenome-derived LC11-RNase H1 in complex with RNA/DNA hybrid" @default.
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- W2080304317 doi "https://doi.org/10.1016/j.jsb.2013.02.018" @default.
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