1orp

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(New page: 200px<br /><applet load="1orp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1orp, resolution 2.20&Aring;" /> '''Structure of a Trapp...)
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[[Image:1orp.gif|left|200px]]<br /><applet load="1orp" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1orp.gif|left|200px]]<br /><applet load="1orp" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1orp, resolution 2.20&Aring;" />
caption="1orp, resolution 2.20&Aring;" />
'''Structure of a Trapped Endonuclease III-DNA Covalent Intermediate: Estranged-Adenine Complex'''<br />
'''Structure of a Trapped Endonuclease III-DNA Covalent Intermediate: Estranged-Adenine Complex'''<br />
==Overview==
==Overview==
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Nearly all cells express proteins that confer resistance to the mutagenic, effects of oxidative DNA damage. The primary defense against the toxicity, of oxidative nucleobase lesions in DNA is the base-excision repair (BER), pathway. Endonuclease III (EndoIII) is a [4Fe-4S] cluster-containing DNA, glycosylase with repair activity specific for oxidized pyrimidine lesions, in duplex DNA. We have determined the crystal structure of a trapped, intermediate that represents EndoIII frozen in the act of repairing DNA., The structure of the protein-DNA complex provides insight into the ability, of EndoIII to recognize and repair a diverse array of oxidatively damaged, bases. This structure also suggests a rationale for the frequent, occurrence in certain human cancers of a specific mutation in the related, DNA repair protein MYH.
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Nearly all cells express proteins that confer resistance to the mutagenic effects of oxidative DNA damage. The primary defense against the toxicity of oxidative nucleobase lesions in DNA is the base-excision repair (BER) pathway. Endonuclease III (EndoIII) is a [4Fe-4S] cluster-containing DNA glycosylase with repair activity specific for oxidized pyrimidine lesions in duplex DNA. We have determined the crystal structure of a trapped intermediate that represents EndoIII frozen in the act of repairing DNA. The structure of the protein-DNA complex provides insight into the ability of EndoIII to recognize and repair a diverse array of oxidatively damaged bases. This structure also suggests a rationale for the frequent occurrence in certain human cancers of a specific mutation in the related DNA repair protein MYH.
==About this Structure==
==About this Structure==
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1ORP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with NA and SF4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ORP OCA].
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1ORP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=SF4:'>SF4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORP OCA].
==Reference==
==Reference==
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Fromme, J.C.]]
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[[Category: Fromme, J C.]]
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[[Category: Verdine, G.L.]]
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[[Category: Verdine, G L.]]
[[Category: NA]]
[[Category: NA]]
[[Category: SF4]]
[[Category: SF4]]
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[[Category: iron-sulfur cluster]]
[[Category: iron-sulfur cluster]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:20:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:48 2008''

Revision as of 12:20, 21 February 2008


1orp, resolution 2.20Å

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Structure of a Trapped Endonuclease III-DNA Covalent Intermediate: Estranged-Adenine Complex

Overview

Nearly all cells express proteins that confer resistance to the mutagenic effects of oxidative DNA damage. The primary defense against the toxicity of oxidative nucleobase lesions in DNA is the base-excision repair (BER) pathway. Endonuclease III (EndoIII) is a [4Fe-4S] cluster-containing DNA glycosylase with repair activity specific for oxidized pyrimidine lesions in duplex DNA. We have determined the crystal structure of a trapped intermediate that represents EndoIII frozen in the act of repairing DNA. The structure of the protein-DNA complex provides insight into the ability of EndoIII to recognize and repair a diverse array of oxidatively damaged bases. This structure also suggests a rationale for the frequent occurrence in certain human cancers of a specific mutation in the related DNA repair protein MYH.

About this Structure

1ORP is a Protein complex structure of sequences from Geobacillus stearothermophilus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of a trapped endonuclease III-DNA covalent intermediate., Fromme JC, Verdine GL, EMBO J. 2003 Jul 1;22(13):3461-71. PMID:12840008[[Category: [4fe-4s] cluster]]

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