2gcl

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2gcl, resolution 2.21Å

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Structure of the Pob3 Middle domain

Overview

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.

About this Structure

2GCL is a Single protein structure of sequence from Saccharomyces cerevisiae with CL as ligand. Full crystallographic information is available from OCA.

Reference

The structure of the yFACT Pob3-M domain, its interaction with the DNA replication factor RPA, and a potential role in nucleosome deposition., VanDemark AP, Blanksma M, Ferris E, Heroux A, Hill CP, Formosa T, Mol Cell. 2006 May 5;22(3):363-74. PMID:16678108

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