1LQG

ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN

1LQG の概要

• エントリーDOI: 10.2210/pdb1lqg/pdb
• 関連するPDBエントリー: 1EUI 1LQJ 1LQM
• 分子名称: URACIL-DNA GLYCOSYLASE, URACIL-DNA GLYCOSYLASE INHIBITOR (3 entities in total)
• 機能のキーワード: glycosylase, inhibitor, dna repair, base excision, complex (hydrolase-inhibitor), hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: P12295
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 70415.71

構造登録者

Saikrishnan, K.,Sagar, M.B.,Ravishankar, R.,Roy, S.,Purnapatre, K.,Handa, P.,Varshney, U.,Vijayan, M. (登録日: 2002-05-10, 公開日: 2002-11-10, 最終更新日: 2024-02-14)

主引用文献

Saikrishnan, K.,Bidya Sagar, M.,Ravishankar, R.,Roy, S.,Purnapatre, K.,Handa, P.,Varshney, U.,Vijayan, M.
Domain closure and action of uracil DNA glycosylase (UDG): structures of new crystal forms containing the Escherichia coli enzyme and a comparative study of the known structures involving UDG.
Acta Crystallogr.,Sect.D, 58:1269-1276, 2002

PubMed Abstract: The structures of a new crystal form of free Escherichia coli uracil DNA glycosylase (UDG), containing four molecules in the asymmetric unit, and two forms of its complex with the proteinaceous inhibitor Ugi, containing two and four crystallographically independent complexes, have been determined. A comparison of these structures and the already known crystal structures containing UDG shows that the enzyme can be considered to be made up of two independently moving structural entities or domains. A detailed study of free and DNA-bound human enzyme strengthens this conclusion. The domains close upon binding to uracil-containing DNA, whereas they do not appear to do so upon binding to Ugi. The comparative study also shows that the mobility of the molecule involves the rigid-body movement of the domains superposed on flexibility within domains.

PubMed: 12136137
DOI: 10.1107/S0907444902009599

実験手法

X-RAY DIFFRACTION (2.9 Å)