2GCJ

Crystal Structure of the Pob3 middle domain

2GCJ の概要

• エントリーDOI: 10.2210/pdb2gcj/pdb
• 分子名称: Hypothetical 63.0 kDa protein in DAK1-ORC1 intergenic region (2 entities in total)
• 機能のキーワード: chromatin, fact, double ph domain, replication
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus: Q04636
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 121365.15

構造登録者

VanDemark, A.P. (登録日: 2006-03-14, 公開日: 2006-05-23, 最終更新日: 2024-04-03)

主引用文献

VanDemark, A.P.,Blanksma, M.,Ferris, E.,Heroux, A.,Hill, C.P.,Formosa, T.
The Structure of the yFACT Pob3-M Domain, Its Interaction with the DNA Replication Factor RPA, and a Potential Role in Nucleosome Deposition.
Mol.Cell, 22:363-374, 2006

PubMed Abstract: We report the crystal structure of the middle domain of the Pob3 subunit (Pob3-M) of S. cerevisiae FACT (yFACT, facilitates chromatin transcription), which unexpectedly adopts an unusual double pleckstrin homology (PH) architecture. A mutation within a conserved surface cluster in this domain causes a defect in DNA replication that is suppressed by mutation of replication protein A (RPA). The nucleosome reorganizer yFACT therefore interacts in a physiologically important way with the central single-strand DNA (ssDNA) binding factor RPA to promote a step in DNA replication. Purified yFACT and RPA display a weak direct physical interaction, although the genetic suppression is not explained by simple changes in affinity between the purified proteins. Further genetic analysis suggests that coordinated function by yFACT and RPA is important during nucleosome deposition. These results support the model that the FACT family has an essential role in constructing nucleosomes during DNA replication, and suggest that RPA contributes to this process.

PubMed: 16678108
DOI: 10.1016/j.molcel.2006.03.025

実験手法

X-RAY DIFFRACTION (2.55 Å)