1MUN

CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI D138N MUTANT

Summary for 1MUN

• Entry DOI: 10.2210/pdb1mun/pdb
• Descriptor: ADENINE GLYCOSYLASE, IRON/SULFUR CLUSTER, IMIDAZOLE, ... (5 entities in total)
• Functional Keywords: dna repair, dna g.a mismatch repair enzyme, glycosidase, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 25837.16

Authors

Guan, Y.,Tainer, J.A. (deposition date: 1998-08-26, release date: 1999-08-26, Last modification date: 2024-04-03)

Primary citation

Guan, 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

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

Experimental method

X-RAY DIFFRACTION (1.2 Å)