1ynx: Difference between revisions
New page: left|200px<br /><applet load="1ynx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ynx" /> '''Solution structure of DNA binding domain A (... |
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[[Image:1ynx.gif|left|200px]]<br /><applet load="1ynx" size=" | [[Image:1ynx.gif|left|200px]]<br /><applet load="1ynx" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''Solution structure of DNA binding domain A (DBD-A) of S.cerevisiae Replication Protein A (RPA)'''<br /> | '''Solution structure of DNA binding domain A (DBD-A) of S.cerevisiae Replication Protein A (RPA)'''<br /> | ||
==Overview== | ==Overview== | ||
Replication protein A (RPA) is a three-subunit complex with multiple roles | Replication protein A (RPA) is a three-subunit complex with multiple roles in DNA metabolism. DNA-binding domain A in the large subunit of human RPA (hRPA70A) binds to single-stranded DNA (ssDNA) and is responsible for the species-specific RPA-T antigen (T-ag) interaction required for Simian virus 40 replication. Although Saccharomyces cerevisiae RPA70A (scRPA70A) shares high sequence homology with hRPA70A, the two are not functionally equivalent. To elucidate the similarities and differences between these two homologous proteins, we determined the solution structure of scRPA70A, which closely resembled the structure of hRPA70A. The structure of ssDNA-bound scRPA70A, as simulated by residual dipolar coupling-based homology modeling, suggested that the positioning of the ssDNA is the same for scRPA70A and hRPA70A, although the conformational changes that occur in the two proteins upon ssDNA binding are not identical. NMR titrations of hRPA70A with T-ag showed that the T-ag binding surface is separate from the ssDNA-binding region and is more neutral than the corresponding part of scRPA70A. These differences might account for the species-specific nature of the hRPA70A-T-ag interaction. Our results provide insight into how these two homologous RPA proteins can exhibit functional differences, but still both retain their ability to bind ssDNA. | ||
==About this Structure== | ==About this Structure== | ||
1YNX 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:// | 1YNX 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=1YNX OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Choi, B | [[Category: Choi, B S.]] | ||
[[Category: Lee, J | [[Category: Lee, J H.]] | ||
[[Category: Park, C | [[Category: Park, C J.]] | ||
[[Category: canonical ob fold]] | [[Category: canonical ob fold]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:18 2008'' | ||
Revision as of 17:07, 21 February 2008
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Solution structure of DNA binding domain A (DBD-A) of S.cerevisiae Replication Protein A (RPA)
OverviewOverview
Replication protein A (RPA) is a three-subunit complex with multiple roles in DNA metabolism. DNA-binding domain A in the large subunit of human RPA (hRPA70A) binds to single-stranded DNA (ssDNA) and is responsible for the species-specific RPA-T antigen (T-ag) interaction required for Simian virus 40 replication. Although Saccharomyces cerevisiae RPA70A (scRPA70A) shares high sequence homology with hRPA70A, the two are not functionally equivalent. To elucidate the similarities and differences between these two homologous proteins, we determined the solution structure of scRPA70A, which closely resembled the structure of hRPA70A. The structure of ssDNA-bound scRPA70A, as simulated by residual dipolar coupling-based homology modeling, suggested that the positioning of the ssDNA is the same for scRPA70A and hRPA70A, although the conformational changes that occur in the two proteins upon ssDNA binding are not identical. NMR titrations of hRPA70A with T-ag showed that the T-ag binding surface is separate from the ssDNA-binding region and is more neutral than the corresponding part of scRPA70A. These differences might account for the species-specific nature of the hRPA70A-T-ag interaction. Our results provide insight into how these two homologous RPA proteins can exhibit functional differences, but still both retain their ability to bind ssDNA.
About this StructureAbout this Structure
1YNX is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the DNA-binding domain of RPA from Saccharomyces cerevisiae and its interaction with single-stranded DNA and SV40 T antigen., Park CJ, Lee JH, Choi BS, Nucleic Acids Res. 2005 Jul 25;33(13):4172-81. Print 2005. PMID:16043636
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