1TFR
RNASE H FROM BACTERIOPHAGE T4
Summary for 1TFR
| Entry DOI | 10.2210/pdb1tfr/pdb |
| Descriptor | T4 RNASE H, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | 5u-3u exonuclease, rna:rna, dna:dna, metal-dependent, magnesium-containing, hydrolase (nucleic acid), hydrolase |
| Biological source | Enterobacteria phage T4 |
| Total number of polymer chains | 1 |
| Total formula weight | 35659.52 |
| Authors | Mueser, T.C.,Nossal, N.G.,Hyde, C.C. (deposition date: 1996-04-27, release date: 1996-11-08, Last modification date: 2024-02-14) |
| Primary citation | Mueser, T.C.,Nossal, N.G.,Hyde, C.C. 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(Cambridge,Mass.), 85:1101-1112, 1996 Cited by PubMed 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. PubMed: 8674116DOI: 10.1016/S0092-8674(00)81310-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.06 Å) |
Structure validation
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