1MUD

CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI, D138N MUTANT COMPLEXED TO ADENINE

1MUD の概要

• エントリーDOI: 10.2210/pdb1mud/pdb
• 分子名称: Adenine DNA glycosylase, IRON/SULFUR CLUSTER, ADENINE, ... (5 entities in total)
• 機能のキーワード: dna repair, dna g.a mismatch repair enzyme, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25761.99

構造登録者

Guan, Y.,Tainer, J.A. (登録日: 1998-08-20, 公開日: 1999-09-20, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)