1T5L

Crystal structure of the DNA repair protein UvrB point mutant Y96A revealing a novel fold for domain 2

1T5L の概要

• エントリーDOI: 10.2210/pdb1t5l/pdb
• 関連するPDBエントリー: 1C40 1D2M 1D9X 1D9Z 1E52 1QOJ
• 分子名称: UvrABC system protein B, ZINC ION (3 entities in total)
• 機能のキーワード: dna damage, dna repair, nucleotide excision repair, uvrb, uvra, uvrc, ner, mfd, trcf, dna excision repair
• 由来する生物種: Bacillus caldotenax
• 細胞内の位置: Cytoplasm (By similarity): P56981
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 151251.45

構造登録者

Truglio, J.J.,Croteau, D.L.,Skorvaga, M.,DellaVecchia, M.J.,Theis, K.,Mandavilli, B.S.,Van Houten, B.,Kisker, C. (登録日: 2004-05-04, 公開日: 2004-06-22, 最終更新日: 2024-02-14)

主引用文献

Truglio, J.J.,Croteau, D.L.,Skorvaga, M.,DellaVecchia, M.J.,Theis, K.,Mandavilli, B.S.,Van Houten, B.,Kisker, C.
Interactions between UvrA and UvrB: the role of UvrB's domain 2 in nucleotide excision repair
Embo J., 23:2498-2509, 2004

PubMed Abstract: Nucleotide excision repair (NER) is a highly conserved DNA repair mechanism present in all kingdoms of life. UvrB is a central component of the bacterial NER system, participating in damage recognition, strand excision and repair synthesis. None of the three presently available crystal structures of UvrB has defined the structure of domain 2, which is critical for the interaction with UvrA. We have solved the crystal structure of the UvrB Y96A variant, which reveals a new fold for domain 2 and identifies highly conserved residues located on its surface. These residues are restricted to the face of UvrB important for DNA binding and may be critical for the interaction of UvrB with UvrA. We have mutated these residues to study their role in the incision reaction, formation of the pre-incision complex, destabilization of short duplex regions in DNA, binding to UvrA and ATP hydrolysis. Based on the structural and biochemical data, we conclude that domain 2 is required for a productive UvrA-UvrB interaction, which is a pre-requisite for all subsequent steps in nucleotide excision repair.

PubMed: 15192705
DOI: 10.1038/sj.emboj.7600263

実験手法

X-RAY DIFFRACTION (2.6 Å)