6O8H

Crystal structure of UvrB mutant bound to duplex DNA

6O8H の概要

• エントリーDOI: 10.2210/pdb6o8h/pdb
• 分子名称: UvrABC system protein B, DNA (5'-D(P*CP*CP*AP*TP*CP*GP*CP*GP*CP*TP*AP*CP*C)-3'), DNA (5'-D(P*AP*GP*CP*GP*CP*GP*AP*TP*GP*GP*AP*GP*A)-3'), ... (6 entities in total)
• 機能のキーワード: dna repair, nucleotide excision repair, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Bacillus caldotenax; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 78142.75

構造登録者

Lee, S.-J.,Verdine, G.L. (登録日: 2019-03-10, 公開日: 2020-01-22, 最終更新日: 2024-03-13)

主引用文献

Lee, S.J.,Sung, R.J.,Verdine, G.L.
Mechanism of DNA Lesion Homing and Recognition by the Uvr Nucleotide Excision Repair System.
Res, 2019:5641746-5641746, 2019

PubMed Abstract: Nucleotide excision repair (NER) is an essential DNA repair system distinguished from other such systems by its extraordinary versatility. NER removes a wide variety of structurally dissimilar lesions having only their bulkiness in common. NER can also repair several less bulky nucleobase lesions, such as 8-oxoguanine. Thus, how a single DNA repair system distinguishes such a diverse array of structurally divergent lesions from undamaged DNA has been one of the great unsolved mysteries in the field of genome maintenance. Here we employ a synthetic crystallography approach to obtain crystal structures of the pivotal NER enzyme UvrB in complex with duplex DNA, trapped at the stage of lesion-recognition. These structures coupled with biochemical studies suggest that UvrB integrates the ATPase-dependent helicase/translocase and lesion-recognition activities. Our work also conclusively establishes the identity of the lesion-containing strand and provides a compelling insight to how UvrB recognizes a diverse array of DNA lesions.

PubMed: 31549070
DOI: 10.34133/2019/5641746

実験手法

X-RAY DIFFRACTION (2.39 Å)