1YNX

Solution structure of DNA binding domain A (DBD-A) of S.cerevisiae Replication Protein A (RPA)

1YNX の概要

• エントリーDOI: 10.2210/pdb1ynx/pdb
• 関連するPDBエントリー: 1fgu 1jmc
• 分子名称: Replication factor-A protein 1 (1 entity in total)
• 機能のキーワード: canonical ob fold, dna binding protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus: P22336
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13265.82

構造登録者

Park, C.J.,Lee, J.H.,Choi, B.S. (登録日: 2005-01-26, 公開日: 2006-01-10, 最終更新日: 2024-05-29)

主引用文献

Park, C.J.,Lee, J.H.,Choi, B.S.
Solution structure of the DNA-binding domain of RPA from Saccharomyces cerevisiae and its interaction with single-stranded DNA and SV40 T antigen
Nucleic Acids Res., 33:4172-4181, 2005

PubMed Abstract: Replication protein A (RPA) is a three-subunit complex with multiple roles in DNA metabolism. DNA-binding domain A in the large subunit of human RPA (hRPA70A) binds to single-stranded DNA (ssDNA) and is responsible for the species-specific RPA-T antigen (T-ag) interaction required for Simian virus 40 replication. Although Saccharomyces cerevisiae RPA70A (scRPA70A) shares high sequence homology with hRPA70A, the two are not functionally equivalent. To elucidate the similarities and differences between these two homologous proteins, we determined the solution structure of scRPA70A, which closely resembled the structure of hRPA70A. The structure of ssDNA-bound scRPA70A, as simulated by residual dipolar coupling-based homology modeling, suggested that the positioning of the ssDNA is the same for scRPA70A and hRPA70A, although the conformational changes that occur in the two proteins upon ssDNA binding are not identical. NMR titrations of hRPA70A with T-ag showed that the T-ag binding surface is separate from the ssDNA-binding region and is more neutral than the corresponding part of scRPA70A. These differences might account for the species-specific nature of the hRPA70A-T-ag interaction. Our results provide insight into how these two homologous RPA proteins can exhibit functional differences, but still both retain their ability to bind ssDNA.

PubMed: 16043636
DOI: 10.1093/nar/gki736

実験手法

SOLUTION NMR