2C2Q

The crystal structure of mismatch specific uracil-DNA glycosylase (MUG) from Deinococcus radiodurans. Inactive mutant Asp93Ala.

2C2Q の概要

• エントリーDOI: 10.2210/pdb2c2q/pdb
• 関連するPDBエントリー: 2C2P
• 分子名称: G/U MISMATCH-SPECIFIC DNA GLYCOSYLASE, ACETATE ION (3 entities in total)
• 機能のキーワード: deinococcus radiodurans, radiation resistance, dna repair enzymes, uracil-dna glycosylase, mismatch specific dna-glycosylase, mug, hydrolase
• 由来する生物種: DEINOCOCCUS RADIODURANS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21800.62

構造登録者

Moe, E.,Leiros, I.,Smalas, A.O.,McSweeney, S. (登録日: 2005-09-29, 公開日: 2005-10-18, 最終更新日: 2023-12-13)

主引用文献

Moe, E.,Leiros, I.,Smalas, A.O.,Mcsweeney, S.
The Crystal Structure of Mismatch Specific Uracil-DNA Glycosylase (Mug) from Deinococcus Radiodurans Reveals a Novel Catalytic Residue and Broad Substrate Specificity
J.Biol.Chem., 281:569-, 2006

PubMed Abstract: Deinococcus radiodurans is extremely resistant to the effects of ionizing radiation. The source of the radiation resistance is not known, but an expansion of specific protein families related to stress response and damage control has been observed. DNA repair enzymes are among the expanded protein families in D. radiodurans, and genes encoding five different uracil-DNA glycosylases are identified in the genome. Here we report the three-dimensional structure of the mismatch-specific uracil-DNA glycosylase (MUG) from D. radiodurans (drMUG) to a resolution of 1.75 angstroms. Structural analyses suggest that drMUG possesses a novel catalytic residue, Asp-93. Activity measurements show that drMUG has a modified and broadened substrate specificity compared with Escherichia coli MUG. The importance of Asp-93 for activity was confirmed by structural analysis and abolished activity for the mutant drMUGD93A. Two other microorganisms, Bradyrhizobium japonicum and Rhodopseudomonas palustris, possess genes that encode MUGs with the highest sequence identity to drMUG among all of the bacterial MUGs examined. A phylogenetic analysis indicates that these three MUGs form a new MUG/thymidine-DNA glycosylase subfamily, here called the MUG2 family. We suggest that the novel catalytic residue (Asp-93) has evolved to provide drMUG with broad substrate specificity to increase the DNA repair repertoire of D. radiodurans.

PubMed: 16223719
DOI: 10.1074/JBC.M508032200

実験手法

X-RAY DIFFRACTION (1.7 Å)