4GOP

Structure and Conformational Change of a Replication Protein A Heterotrimer Bound to ssDNA

4GOP の概要

• エントリーDOI: 10.2210/pdb4gop/pdb
• 分子名称: Putative uncharacterized protein, DNA (25-MER), ZINC ION, ... (5 entities in total)
• 機能のキーワード: ob fold, ssdna binding, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Ustilago maydis (Smut fungus); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 174031.82

構造登録者

Pavletich, N.P.,Jie, F. (登録日: 2012-08-20, 公開日: 2012-11-28, 最終更新日: 2024-11-06)

主引用文献

Fan, J.,Pavletich, N.P.
Structure and conformational change of a replication protein A heterotrimer bound to ssDNA.
Genes Dev., 26:2337-2347, 2012

PubMed Abstract: Replication protein A (RPA) is the main eukaryotic ssDNA-binding protein with essential roles in DNA replication, recombination, and repair. RPA maintains the DNA as single-stranded and also interacts with other DNA-processing proteins, coordinating their assembly and disassembly on DNA. RPA binds to ssDNA in two conformational states with opposing affinities for DNA and proteins. The RPA-protein interactions are compatible with a low DNA affinity state that involves DNA-binding domain A (DBD-A) and DBD-B but not with the high DNA affinity state that additionally engages DBD-C and DBD-D. The structure of the high-affinity RPA-ssDNA complex reported here shows a compact quaternary structure held together by a four-way interface between DBD-B, DBD-C, the intervening linker (BC linker), and ssDNA. The BC linker binds into the DNA-binding groove of DBD-B, mimicking DNA. The associated conformational change and partial occlusion of the DBD-A-DBA-B protein-protein interaction site establish a mechanism for the allosteric coupling of RPA-DNA and RPA-protein interactions.

PubMed: 23070815
DOI: 10.1101/gad.194787.112

実験手法

X-RAY DIFFRACTION (3.1 Å)