1FGU

SSDNA-BINDING DOMAIN OF THE LARGE SUBUNIT OF REPLICATION PROTEIN A

1FGU の概要

• エントリーDOI: 10.2210/pdb1fgu/pdb
• 関連するPDBエントリー: 1jmc
• 分子名称: REPLICATION PROTEIN A 70 KDA DNA-BINDING SUBUNIT (2 entities in total)
• 機能のキーワード: ob-fold, ssdna-binding protein, replication
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56219.28

構造登録者

Bochkareva, E.,Belegu, V.,Korolev, S.,Bochkarev, A. (登録日: 2000-07-28, 公開日: 2001-02-07, 最終更新日: 2024-02-07)

主引用文献

Bochkareva, E.,Belegu, V.,Korolev, S.,Bochkarev, A.
Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding.
EMBO J., 20:612-618, 2001

PubMed Abstract: Although structures of single-stranded (ss)DNA-binding proteins (SSBs) have been reported with and without ssDNA, the mechanism of ssDNA binding in eukarya remains speculative. Here we report a 2.5 Angstroms structure of the ssDNA-binding domain of human replication protein A (RPA) (eukaryotic SSB), for which we previously reported a structure in complex with ssDNA. A comparison of free and bound forms of RPA revealed that ssDNA binding is associated with a major reorientation between, and significant conformational changes within, the structural modules--OB-folds--which comprise the DNA-binding domain. Two OB-folds, whose tandem orientation was stabilized by the presence of DNA, adopted multiple orientations in its absence. Within the OB-folds, extended loops implicated in DNA binding significantly changed conformation in the absence of DNA. Analysis of intermolecular contacts suggested the possibility that other RPA molecules and/or other proteins could compete with DNA for the same binding site. Using this mechanism, protein-protein interactions can regulate, and/or be regulated by DNA binding. Combined with available biochemical data, this structure also suggested a dynamic model for the DNA-binding mechanism.

PubMed: 11157767
DOI: 10.1093/emboj/20.3.612

実験手法

X-RAY DIFFRACTION (2.5 Å)