1kea

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[[Image:1kea.jpg|left|200px]]
[[Image:1kea.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1kea", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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{{STRUCTURE_1kea| PDB=1kea | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kea OCA], [http://www.ebi.ac.uk/pdbsum/1kea PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kea RCSB]</span>
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'''STRUCTURE OF A THERMOSTABLE THYMINE-DNA GLYCOSYLASE'''
'''STRUCTURE OF A THERMOSTABLE THYMINE-DNA GLYCOSYLASE'''
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[[Category: Mol, C D.]]
[[Category: Mol, C D.]]
[[Category: Tainer, J A.]]
[[Category: Tainer, J A.]]
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[[Category: base twisting]]
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[[Category: Base twisting]]
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[[Category: dna glycosylase]]
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[[Category: Dna glycosylase]]
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[[Category: dna mismatch]]
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[[Category: Dna mismatch]]
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[[Category: dna repair]]
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[[Category: Dna repair]]
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[[Category: methylation]]
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[[Category: Methylation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:38:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:47:21 2008''
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Revision as of 19:38, 2 May 2008

Image:1kea.jpg

Template:STRUCTURE 1kea

STRUCTURE OF A THERMOSTABLE THYMINE-DNA GLYCOSYLASE


Overview

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.

About this Structure

1KEA is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

Reference

Structure and activity of a thermostable thymine-DNA glycosylase: evidence for base twisting to remove mismatched normal DNA bases., Mol CD, Arvai AS, Begley TJ, Cunningham RP, Tainer JA, J Mol Biol. 2002 Jan 18;315(3):373-84. PMID:11786018 Page seeded by OCA on Fri May 2 22:38:13 2008

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