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 2.06&Aring;" /> '''RNASE H FROM BACTERI...)
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[[Image:1tfr.gif|left|200px]]<br /><applet load="1tfr" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1tfr.gif|left|200px]]<br /><applet load="1tfr" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1tfr, resolution 2.06&Aring;" />
caption="1tfr, resolution 2.06&Aring;" />
'''RNASE H FROM BACTERIOPHAGE T4'''<br />
'''RNASE H FROM BACTERIOPHAGE T4'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1TFR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TFR OCA].
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1TFR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFR OCA].
==Reference==
==Reference==
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[[Category: Ribonuclease H]]
[[Category: Ribonuclease H]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hyde, C.C.]]
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[[Category: Hyde, C C.]]
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[[Category: Mueser, T.C.]]
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[[Category: Mueser, T C.]]
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[[Category: Nossal, N.G.]]
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[[Category: Nossal, N G.]]
[[Category: MG]]
[[Category: MG]]
[[Category: 5u-3u exonuclease]]
[[Category: 5u-3u exonuclease]]
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[[Category: rna:rna]]
[[Category: rna:rna]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:13:46 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:04 2008''

Revision as of 13:13, 21 February 2008


1tfr, resolution 2.06Å

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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 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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