1ynx
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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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