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1tfr
From Proteopedia
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| , resolution 2.06Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Ribonuclease H, with EC number 3.1.26.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RNASE H FROM BACTERIOPHAGE T4
Overview
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.
About this Structure
1TFR is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
Reference
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., Mueser TC, Nossal NG, Hyde CC, Cell. 1996 Jun 28;85(7):1101-12. PMID:8674116
Page seeded by OCA on Thu Mar 20 14:17:48 2008
