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1l2c
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(New page: 200px<br /><applet load="1l2c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l2c, resolution 2.2Å" /> '''MutM (Fpg)-DNA Estran...)
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Revision as of 00:15, 25 November 2007
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MutM (Fpg)-DNA Estranged Thymine Mismatch Recognition Complex
Overview
MutM is a bacterial 8-oxoguanine glycosylase responsible for initiating, base-excision repair of oxidized guanine residues in DNA. Here we report, five different crystal structures of MutM-DNA complexes that represent, different steps of the repair reaction cascade catalyzed by the protein, and also differ in the identity of the base opposite the lesion (the, 'estranged' base). These structures reveal that the MutM active site, performs the multiple steps of base-excision and 3' and 5' nicking with, minimal rearrangement of the DNA backbone.
About this Structure
1L2C is a Protein complex structure of sequences from Geobacillus stearothermophilus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM., Fromme JC, Verdine GL, Nat Struct Biol. 2002 Jul;9(7):544-52. PMID:12055620
Page seeded by OCA on Sun Nov 25 02:22:55 2007
