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| {{STRUCTURE_1kea| PDB=1kea | SCENE= }} | | {{STRUCTURE_1kea| PDB=1kea | SCENE= }} |
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| '''STRUCTURE OF A THERMOSTABLE THYMINE-DNA GLYCOSYLASE'''
| | ===STRUCTURE OF A THERMOSTABLE THYMINE-DNA GLYCOSYLASE=== |
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| ==Overview==
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| The repair of T:G mismatches in DNA is key for maintaining bacterial restriction/modification systems and gene silencing in higher eukaryotes. T:G mismatch repair can be initiated by a specific mismatch glycosylase (MIG) that is homologous to the helix-hairpin-helix (HhH) DNA repair enzymes. Here, we present a 2.0 A resolution crystal structure and complementary mutagenesis results for this thermophilic HhH MIG enzyme. The results suggest that MIG distorts the target thymine nucleotide by twisting the thymine base approximately 90 degrees away from its normal anti position within DNA. We propose that functionally significant differences exist in DNA repair enzyme extrahelical nucleotide binding and catalysis that are characteristic of whether the target base is damaged or is a normal base within a mispair. These results explain why pure HhH DNA glycosylases and combined glycosylase/AP lyases cannot be interconverted by simply altering their functional group chemistry, and how broad-specificity DNA glycosylase enzymes may weaken the glycosylic linkage to allow a variety of damaged DNA bases to be excised. | | The line below this paragraph, {{ABSTRACT_PUBMED_11786018}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11786018 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11786018}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Dna repair]] | | [[Category: Dna repair]] |
| [[Category: Methylation]] | | [[Category: Methylation]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:38:13 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:12:37 2008'' |
