5X55

Crystal structure of mimivirus uracil-DNA glycosylase

5X55 の概要

• エントリーDOI: 10.2210/pdb5x55/pdb
• 分子名称: Probable uracil-DNA glycosylase (2 entities in total)
• 機能のキーワード: family-i uracil-dna glycosylase, long n-domain, insertional motif, hydrolase
• 由来する生物種: Acanthamoeba polyphaga mimivirus (APMV)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84553.95

構造登録者

Kwon, E.,Pathak, D.,Kim, D.Y. (登録日: 2017-02-14, 公開日: 2017-08-09, 最終更新日: 2024-11-13)

主引用文献

Kwon, E.,Pathak, D.,Chang, H.W.,Kim, D.Y.
Crystal structure of mimivirus uracil-DNA glycosylase
PLoS ONE, 12:e0182382-e0182382, 2017

PubMed Abstract: Cytosine deamination induced by stresses or enzymatic catalysis converts deoxycytidine into deoxyuridine, thereby introducing a G to A mutation after DNA replication. Base-excision repair to correct uracil to cytosine is initiated by uracil-DNA glycosylase (UDG), which recognizes and eliminates uracil from DNA. Mimivirus, one of the largest known viruses, also encodes a distinctive UDG gene containing a long N-terminal domain (N-domain; residues 1-130) and a motif-I (residues 327-343), in addition to the canonical catalytic domain of family I UDGs (also called UNGs). To understand the structural and functional features of the additional segments, we have determined the crystal structure of UNG from Acanthamoeba polyphaga mimivirus (mvUNG). In the crystal structure of mvUNG, residues 95-130 in the N-domain bind to a hydrophobic groove in the catalytic domain, and motif-I forms a short β-sheet with a positively charged surface near the active site. Circular dichroism spectra showed that residues 1-94 are in a random coil conformation. Deletion of the three additional fragments reduced the activity and thermal stability, compared to full-length mvUNG. The results suggested that the mvUNG N-domain and motif-I are required for its structural and functional integrity.

PubMed: 28763516
DOI: 10.1371/journal.pone.0182382

実験手法

X-RAY DIFFRACTION (2.302 Å)