1tfr

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|PDB= 1tfr |SIZE=350|CAPTION= <scene name='initialview01'>1tfr</scene>, resolution 2.06&Aring;
|PDB= 1tfr |SIZE=350|CAPTION= <scene name='initialview01'>1tfr</scene>, resolution 2.06&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tfr OCA], [http://www.ebi.ac.uk/pdbsum/1tfr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tfr RCSB]</span>
}}
}}
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==About this Structure==
==About this Structure==
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1TFR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFR OCA].
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1TFR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFR OCA].
==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/8674116 8674116]
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:[http://www.ncbi.nlm.nih.gov/pubmed/8674116 8674116]
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[[Category: Bacteriophage t4]]
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[[Category: Enterobacteria phage t4]]
[[Category: Ribonuclease H]]
[[Category: Ribonuclease H]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Mueser, T C.]]
[[Category: Mueser, T C.]]
[[Category: Nossal, N G.]]
[[Category: Nossal, N G.]]
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[[Category: MG]]
 
[[Category: 5u-3u exonuclease]]
[[Category: 5u-3u exonuclease]]
[[Category: dna:dna]]
[[Category: dna:dna]]
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[[Category: rna:rna]]
[[Category: rna:rna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:17:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:27 2008''

Revision as of 20:55, 30 March 2008


PDB ID 1tfr

Drag the structure with the mouse to rotate
, resolution 2.06Å
Ligands:
Activity: Ribonuclease H, with EC number 3.1.26.4
Resources: FirstGlance, OCA, PDBsum, RCSB
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 Enterobacteria phage 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

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