2GCL

Structure of the Pob3 Middle domain

Summary for 2GCL

• Entry DOI: 10.2210/pdb2gcl/pdb
• Related: 2GCJ
• Descriptor: Hypothetical 63.0 kDa protein in DAK1-ORC1 intergenic region, CHLORIDE ION (3 entities in total)
• Functional Keywords: chromaint, double ph domain, yfact, dna replication, rpa, replication
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: Q04636
• Total number of polymer chains: 2
• Total formula weight: 61399.46

Authors

VanDemark, A.P. (deposition date: 2006-03-14, release date: 2006-05-23, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.21 Å)