DNA glycosylase
From Proteopedia
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<StructureSection load='3fsp' size='340' side='right' caption='Adenine DNA glycosylate complex with DNA, Fe4-S4 cluster, phosphoric acid esther and Ca+2 ion (PDB code [[3fsp]]).' scene=''> | <StructureSection load='3fsp' size='340' side='right' caption='Adenine DNA glycosylate complex with DNA, Fe4-S4 cluster, phosphoric acid esther and Ca+2 ion (PDB code [[3fsp]]).' scene=''> | ||
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'''DNA glycosylase''' (DG) are enzymes which remove damaged DNA bases by flipping them out of the double helix followed by their cleavage. Monofunctional DG have only glycosylase activity; bifunctional DG also act as lysates; ADG, UDG, TDG remove adenine, uracil, thymine from DNA.<br /> | '''DNA glycosylase''' (DG) are enzymes which remove damaged DNA bases by flipping them out of the double helix followed by their cleavage. Monofunctional DG have only glycosylase activity; bifunctional DG also act as lysates; ADG, UDG, TDG remove adenine, uracil, thymine from DNA.<br /> | ||
| - | * '''Adenine DNA glycosylase''' is also called '''MutY'''.<br /> | + | * '''Adenine DNA glycosylase''' is also called '''MutY'''. MutY has a role in prevention of DNA mutations resulting from oxidative damage forming the mutated base oxoG. DNA polymerase misreads oxoG and pairs it with adenine instead of cytosine. MutY removes adenine from the mismatched oxoG:A pair. MutY contains a 4Fe4S cluster.<br /> |
* '''Thymine DNA glycosylase''' removes thymine moieties from mismatched G/T, C/T and T/T.<br /> | * '''Thymine DNA glycosylase''' removes thymine moieties from mismatched G/T, C/T and T/T.<br /> | ||
* '''Smug1''' is a single-strand selective monofunctional UDG. <br /> | * '''Smug1''' is a single-strand selective monofunctional UDG. <br /> | ||
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*[[Fpg Nei Protein Family]]<br /> | *[[Fpg Nei Protein Family]]<br /> | ||
*[[Fpg Nei Protein Superfamily]]. | *[[Fpg Nei Protein Superfamily]]. | ||
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| + | == Structural highlights == | ||
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| + | MutY uses base flipping to twist the mispaired adenine out of the DNA helix and into the MutY active site. MutY contains 2 domains: C-terminal domain and catalytic domain containing a helix-hairpin-helix. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:16, 1 December 2015
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3D Structures of DNA glycosylate
Updated on 01-December-2015
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
