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1MUN

CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI D138N MUTANT

Summary for 1MUN
Entry DOI10.2210/pdb1mun/pdb
DescriptorADENINE GLYCOSYLASE, IRON/SULFUR CLUSTER, IMIDAZOLE, ... (5 entities in total)
Functional Keywordsdna repair, dna g.a mismatch repair enzyme, glycosidase, hydrolase
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight25837.16
Authors
Guan, Y.,Tainer, J.A. (deposition date: 1998-08-26, release date: 1999-08-26, Last modification date: 2024-04-03)
Primary citationGuan, Y.,Manuel, R.C.,Arvai, A.S.,Parikh, S.S.,Mol, C.D.,Miller, J.H.,Lloyd, S.,Tainer, J.A.
MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily.
Nat.Struct.Biol., 5:1058-1064, 1998
Cited by
PubMed Abstract: 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.
PubMed: 9846876
DOI: 10.1038/4168
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.2 Å)
Structure validation

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