1rrq
From Proteopedia
(New page: 200px<br /><applet load="1rrq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rrq, resolution 2.22Å" /> '''MutY adenine glycosy...) |
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| - | [[Image:1rrq.gif|left|200px]]<br /><applet load="1rrq" size=" | + | [[Image:1rrq.gif|left|200px]]<br /><applet load="1rrq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rrq, resolution 2.22Å" /> | caption="1rrq, resolution 2.22Å" /> | ||
'''MutY adenine glycosylase in complex with DNA containing an A:oxoG pair'''<br /> | '''MutY adenine glycosylase in complex with DNA containing an A:oxoG pair'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The genomes of aerobic organisms suffer chronic oxidation of guanine to | + | The genomes of aerobic organisms suffer chronic oxidation of guanine to the genotoxic product 8-oxoguanine (oxoG). Replicative DNA polymerases misread oxoG residues and insert adenine instead of cytosine opposite the oxidized base. Both bases in the resulting A*oxoG mispair are mutagenic lesions, and both must undergo base-specific replacement to restore the original C*G pair. Doing so represents a formidable challenge to the DNA repair machinery, because adenine makes up roughly 25% of the bases in most genomes. The evolutionarily conserved enzyme adenine DNA glycosylase (called MutY in bacteria and hMYH in humans) initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. A central issue concerning MutY function is the mechanism by which A*oxoG mispairs are targeted among the vast excess of A*T pairs. Here we report the use of disulphide crosslinking to obtain high-resolution crystal structures of MutY-DNA lesion-recognition complexes. These structures reveal the basis for recognizing both lesions in the A*oxoG pair and for catalysing removal of the adenine base. |
==About this Structure== | ==About this Structure== | ||
| - | 1RRQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with CA and SF4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RRQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=CA:'>CA</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=1RRQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Banerjee, A.]] | [[Category: Banerjee, A.]] | ||
| - | [[Category: Fromme, J | + | [[Category: Fromme, J C.]] |
| - | [[Category: Huang, S | + | [[Category: Huang, S J.]] |
| - | [[Category: Verdine, G | + | [[Category: Verdine, G L.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: SF4]] | [[Category: SF4]] | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:52 2008'' |
Revision as of 12:53, 21 February 2008
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MutY adenine glycosylase in complex with DNA containing an A:oxoG pair
Overview
The genomes of aerobic organisms suffer chronic oxidation of guanine to the genotoxic product 8-oxoguanine (oxoG). Replicative DNA polymerases misread oxoG residues and insert adenine instead of cytosine opposite the oxidized base. Both bases in the resulting A*oxoG mispair are mutagenic lesions, and both must undergo base-specific replacement to restore the original C*G pair. Doing so represents a formidable challenge to the DNA repair machinery, because adenine makes up roughly 25% of the bases in most genomes. The evolutionarily conserved enzyme adenine DNA glycosylase (called MutY in bacteria and hMYH in humans) initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. A central issue concerning MutY function is the mechanism by which A*oxoG mispairs are targeted among the vast excess of A*T pairs. Here we report the use of disulphide crosslinking to obtain high-resolution crystal structures of MutY-DNA lesion-recognition complexes. These structures reveal the basis for recognizing both lesions in the A*oxoG pair and for catalysing removal of the adenine base.
About this Structure
1RRQ is a Single protein structure of sequence from Geobacillus stearothermophilus with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase., Fromme JC, Banerjee A, Huang SJ, Verdine GL, Nature. 2004 Feb 12;427(6975):652-6. PMID:14961129
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