1D9Z

CRYSTAL STRUCTURE OF THE DNA REPAIR PROTEIN UVRB IN COMPLEX WITH ATP

1D9Z の概要

• エントリーDOI: 10.2210/pdb1d9z/pdb
• 関連するPDBエントリー: 1D9X
• 分子名称: EXCINUCLEASE UVRABC COMPONENT UVRB, MAGNESIUM ION, ZINC ION, ... (4 entities in total)
• 機能のキーワード: atp-bound protein, excinuclease, gene regulation
• 由来する生物種: Bacillus caldotenax
• 細胞内の位置: Cytoplasm : P56981
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 76092.18

構造登録者

Theis, K.,Chen, P.J.,Skorvaga, M.,Van Houten, B.,Kisker, C. (登録日: 1999-10-30, 公開日: 2000-05-03, 最終更新日: 2024-02-07)

主引用文献

Theis, K.,Chen, P.J.,Skorvaga, M.,Van Houten, B.,Kisker, C.
Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair.
EMBO J., 18:6899-6907, 1999

PubMed Abstract: Nucleotide excision repair (NER) is a highly conserved DNA repair mechanism. NER systems recognize the damaged DNA strand, cleave it on both sides of the lesion, remove and newly synthesize the fragment. UvrB is a central component of the bacterial NER system participating in damage recognition, strand excision and repair synthesis. We have solved the crystal structure of UvrB in the apo and the ATP-bound forms. UvrB contains two domains related in structure to helicases, and two additional domains unique to repair proteins. The structure contains all elements of an intact helicase, and is evidence that UvrB utilizes ATP hydrolysis to move along the DNA to probe for damage. The location of conserved residues and structural comparisons allow us to predict the path of the DNA and suggest that the tight pre-incision complex of UvrB and the damaged DNA is formed by insertion of a flexible beta-hairpin between the two DNA strands.

PubMed: 10601012
DOI: 10.1093/emboj/18.24.6899

実験手法

X-RAY DIFFRACTION (3.15 Å)