1muy
From Proteopedia
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| , resolution 1.4Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI
Overview
The DNA glycosylase MutY, which is a member of the Helix-hairpin-Helix (HhH) DNA glycosylase superfamily, excises adenine from mispairs with 8-oxoguanine and guanine. High-resolution crystal structures of the MutY catalytic core (cMutY), the complex with bound adenine, and designed mutants reveal the basis for adenine specificity and glycosyl bond cleavage chemistry. The two cMutY helical domains form a positively-charged groove with the adenine-specific pocket at their interface. The Watson-Crick hydrogen bond partners of the bound adenine are substituted by protein atoms, confirming a nucleotide flipping mechanism, and supporting a specific DNA binding orientation by MutY and structurally related DNA glycosylases.
About this Structure
1MUY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily., Guan Y, Manuel RC, Arvai AS, Parikh SS, Mol CD, Miller JH, Lloyd S, Tainer JA, Nat Struct Biol. 1998 Dec;5(12):1058-64. PMID:9846876
Page seeded by OCA on Sun Mar 30 22:21:27 2008
