1L1O

Structure of the human Replication Protein A (RPA) trimerization core

1L1O の概要

• エントリーDOI: 10.2210/pdb1l1o/pdb
• 関連するPDBエントリー: 1dpu 1fgu 1jmc 1quq
• 分子名称: Replication protein A 14 kDa subunit, Replication protein A 32 kDa subunit, Replication protein A 70 kDa DNA-binding subunit, ... (4 entities in total)
• 機能のキーワード: eukaryotic ssb, ssdna binding protein, ob-fold, dna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P35244 P15927 P27694
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 98312.97

構造登録者

Bochkareva, E.V.,Korolev, S.,Lees-Miller, S.P.,Bochkarev, A. (登録日: 2002-02-19, 公開日: 2002-06-05, 最終更新日: 2024-02-14)

主引用文献

Bochkareva, E.,Korolev, S.,Lees-Miller, S.P.,Bochkarev, A.
Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA.
EMBO J., 21:1855-1863, 2002

PubMed Abstract: The human single-stranded DNA-binding protein, replication protein A (RPA) binds DNA in at least two different modes: initial [8-10 nucleotides (nt)] and stable ( approximately 30 nt). Switching from 8 to 30 nt mode is associated with a large conformational change. Here we report the 2.8 A structure of the RPA trimerization core comprising the C-terminal DNA-binding domain of subunit RPA70 (DBD-C), the central DNA-binding domain of subunit RPA32 (DBD-D) and the entire RPA14 subunit. All three domains are built around a central oligonucleotide/oligosaccharide binding (OB)-fold and flanked by a helix at the C-terminus. Trimerization is mediated by three C-terminal helices arranged in parallel. The OB-fold of DBD-C possesses unique structural features; embedded zinc ribbon and helix-turn-helix motifs. Using time-resolved proteolysis with trypsin, we demonstrate that the trimerization core does not contribute to the binding with substrates of 10 nt, but interacts with oligonucleotides of 24 nt. Taken together, our data indicate that switching from 8-10 to 30 nt mode is mediated by DNA binding with the trimerization core.

PubMed: 11927569
DOI: 10.1093/emboj/21.7.1855

実験手法

X-RAY DIFFRACTION (2.8 Å)