6Q0C

MutY adenine glycosylase bound to DNA containing a transition state analog (1N) paired with undamaged dG

「3FSP」から置き換えられました

6Q0C の概要

• エントリーDOI: 10.2210/pdb6q0c/pdb
• 関連するPDBエントリー: 6U7T
• 分子名称: A/G-specific adenine glycosylase, DNA (5'-D(*AP*AP*GP*AP*CP*GP*TP*GP*GP*AP*C)-3'), DNA (5'-D(P*GP*TP*CP*CP*AP*(NR1)P*GP*TP*CP*T)-3'), ... (7 entities in total)
• 機能のキーワード: protein-dna complex, dna repair, transition state analog, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Geobacillus stearothermophilus; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 48862.76

構造登録者

O'Shea Murray, V.L.,Russelburg, L.P.,Horvath, M.P.,David, S.S. (登録日: 2019-08-01, 公開日: 2019-08-28, 最終更新日: 2023-10-11)

主引用文献

Russelburg, L.P.,O'Shea Murray, V.L.,Demir, M.,Knutsen, K.R.,Sehgal, S.L.,Cao, S.,David, S.S.,Horvath, M.P.
Structural Basis for Finding OG Lesions and Avoiding Undamaged G by the DNA Glycosylase MutY.
Acs Chem.Biol., 15:93-102, 2020

PubMed Abstract: The adenine glycosylase MutY selectively initiates repair of OG:A lesions and, by comparison, avoids G:A mispairs. The ability to distinguish these closely related substrates relies on the C-terminal domain of MutY, which structurally resembles MutT. To understand the mechanism for substrate specificity, we crystallized MutY in complex with DNA containing G across from the high-affinity azaribose transition state analogue. Our structure shows that G is accommodated by the OG site and highlights the role of a serine residue in OG versus G discrimination. The functional significance of Ser308 and its neighboring residues was evaluated by mutational analysis, revealing the critical importance of a β loop in the C-terminal domain for mutation suppression in cells, and biochemical performance . This loop comprising residues Phe307, Ser308, and His309 ( sequence positions) is conserved in MutY but absent in MutT and other DNA repair enzymes and may therefore serve as a MutY-specific target exploitable by chemical biological probes.

PubMed: 31829624
DOI: 10.1021/acschembio.9b00639

実験手法

X-RAY DIFFRACTION (2 Å)