2c2q
From Proteopedia
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THE CRYSTAL STRUCTURE OF MISMATCH SPECIFIC URACIL-DNA GLYCOSYLASE (MUG) FROM DEINOCOCCUS RADIODURANS. INACTIVE MUTANT ASP93ALA.
Overview
Deinococcus radiodurans is extremely resistant to the effects of ionizing, radiation. The source of the radiation resistance is not known, but an, expansion of specific protein families related to stress response and, damage control has been observed. DNA repair enzymes are among the, expanded protein families in D. radiodurans, and genes encoding five, different uracil-DNA glycosylases are identified in the genome. Here we, report the three-dimensional structure of the mismatch-specific uracil-DNA, glycosylase (MUG) from D. radiodurans (drMUG) to a resolution of 1.75, angstroms. Structural analyses suggest that drMUG possesses a novel, catalytic residue, Asp-93. Activity measurements show that drMUG has a, modified and broadened substrate specificity compared with Escherichia, coli MUG. ... [(full description)]
About this Structure
2C2Q is a [Single protein] structure of sequence from [Deinococcus radiodurans] with ACT as [ligand]. Full crystallographic information is available from [OCA].
Reference
The crystal structure of mismatch-specific uracil-DNA glycosylase (MUG) from Deinococcus radiodurans reveals a novel catalytic residue and broad substrate specificity., Moe E, Leiros I, Smalas AO, McSweeney S, J Biol Chem. 2006 Jan 6;281(1):569-77. Epub 2005 Oct 12. PMID:16223719
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