SGD Paper 
Mueser TC, et al. (1996) Structure of bacteriophage T4 RNase H, a 5' to 3' RNA-DNA and DNA-DNA exonuclease with sequence similarity to the RAD2 family of eukaryotic proteins. Cell 85(7):1101-12
Abstract: Bacteriophage T4 RNase H is a 5' to 3' exonuclease that removes RNA primers from the lagging strand of the DNA replication fork and is a member of the RAD2 family of eukaryotic and prokaryotic replication and repair nucleases. The crystal structure of the full-length native form of T4 RNase H has been solved at 2.06 angstroms resolution in the presence of Mg2+ but in the absence of nucleic acids. The most conserved residues are clustered together in a large cleft with two Mg2+ in the proposed active site. This structure suggests the way in which the widely separated conserved regions in the larger nucleotide excision repair proteins, such as human XPG, could assemble into a structure like that of the smaller replication nucleases.
| Status: Published | Type: Journal Article | PubMed ID: 8674116 |
Topics addressed in this paper
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| Topics | Genes linked to topics |
|---|---|
| RAD2 | |
| Additional Literature |  |
| Non-Fungal Related Genes/Proteins | |
| Protein Sequence Features | |
