1tfr
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(New page: 200px<br /><applet load="1tfr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tfr, resolution 2.06Å" /> '''RNASE H FROM BACTERI...)
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Revision as of 01:06, 21 November 2007
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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 with MG as ligand. Active as Ribonuclease H, with EC number 3.1.26.4 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
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