BACILLUS HALODURANS RNASE H MUTANT D132N IN COMPLEX WITH 12-MER FRNA/DNA HYBRIDBACILLUS HALODURANS RNASE H MUTANT D132N IN COMPLEX WITH 12-MER FRNA/DNA HYBRID

Structural highlights

5swm is a 4 chain structure with sequence from "bacillus_alcalophilus_subsp._halodurans"_boyer_et_al._1973 "bacillus alcalophilus subsp. halodurans" boyer et al. 1973. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
NonStd Res:, , , ,
Gene:rnhA ("Bacillus alcalophilus subsp. halodurans" Boyer et al. 1973)
Activity:Ribonuclease H, with EC number 3.1.26.4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RNH1_BACHD] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.

Publication Abstract from PubMed

RNase H1 cleaves the RNA strand of RNA:DNA hybrids. Replacement of RNA 2'-hydroxyls by fluorine (FRNA) is commonly used to stabilize aptamers and siRNAs. However, FRNA:DNA hybrids fail to elicit RNase H activity. The underlying reasons are unclear, as 2'-OH groups are not directly involved in cleavage. We determined the crystal structure of Bacillus halodurans RNase H bound to a FRNA:DNA hybrid. The structure points to dynamic (slippage of the FRNA:DNA hybrid relative to the enzyme), geometric (different curvatures of FRNA:DNA and RNA:DNA hybrids), and electronic reasons (Mg2+ absent from the active site of the FRNA:DNA complex) for the loss of RNaseH activity.

Limits of RNA 2'-OH Mimicry by Fluorine: Crystal Structure of Bacillus halodurans RNase H Bound to a 2'-FRNA:DNA Hybrid.,Pallan PS, Prakash TP, de Leon AR, Egli M Biochemistry. 2016 Sep 14. PMID:27611889[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Pallan PS, Prakash TP, de Leon AR, Egli M. Limits of RNA 2'-OH Mimicry by Fluorine: Crystal Structure of Bacillus halodurans RNase H Bound to a 2'-FRNA:DNA Hybrid. Biochemistry. 2016 Sep 14. PMID:27611889 doi:http://dx.doi.org/10.1021/acs.biochem.6b00849

5swm, resolution 1.50Å

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