2gcl

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{{STRUCTURE_2gcl| PDB=2gcl | SCENE= }}
{{STRUCTURE_2gcl| PDB=2gcl | SCENE= }}
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'''Structure of the Pob3 Middle domain'''
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===Structure of the Pob3 Middle domain===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_16678108}}
==About this Structure==
==About this Structure==
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[[Category: Rpa]]
[[Category: Rpa]]
[[Category: Yfact]]
[[Category: Yfact]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:32:59 2008''

Revision as of 17:33, 28 July 2008

Image:2gcl.png

Template:STRUCTURE 2gcl

Structure of the Pob3 Middle domain

Template:ABSTRACT PUBMED 16678108

About this Structure

2GCL is a Single protein structure of sequence from Saccharomyces cerevisiae. 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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