2gcj
From Proteopedia
(New page: 200px<br /><applet load="2gcj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gcj, resolution 2.55Å" /> '''Crystal Structure of...) |
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| - | [[Image:2gcj.gif|left|200px]]<br /><applet load="2gcj" size=" | + | [[Image:2gcj.gif|left|200px]]<br /><applet load="2gcj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2gcj, resolution 2.55Å" /> | caption="2gcj, resolution 2.55Å" /> | ||
'''Crystal Structure of the Pob3 middle domain'''<br /> | '''Crystal Structure of the Pob3 middle domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report the crystal structure of the middle domain of the Pob3 subunit | + | 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== | ==About this Structure== | ||
| - | 2GCJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 2GCJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GCJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: VanDemark, A | + | [[Category: VanDemark, A P.]] |
[[Category: chromatin]] | [[Category: chromatin]] | ||
[[Category: double ph domain]] | [[Category: double ph domain]] | ||
[[Category: fact]] | [[Category: fact]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:30:24 2008'' |
Revision as of 15:30, 21 February 2008
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Crystal 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
2GCJ 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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