Crystal structure of an archaeal specific DNA-binding protein (Ape10b2) from Aeropyrum pernix K1 |
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Authors: | Kumarevel Thirumananseri Sakamoto Keiko Gopinath Subash C B Shinkai Akeo Kumar Penmetcha K R Yokoyama Shigeyuki |
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Institution: | RIKEN SPring-8 Center, Harima Institute, Sayo, Hyogo 679-5148, Japan. tskvel@spring8.or.jp |
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Abstract: | DNA binding proteins are essential in all organisms, and they play important roles in both compacting and regulating the genetic material. All thermophilic and hyperthermophilic archaea encode one or more copies of Alba or Sso10b, which is a small, abundant, basic protein that binds DNA. Here, we present the crystal structure of Ape10b2 from Aeropyrum pernix K1 at 1.70 A. Although the overall structure resembles the known Alba protein fold, a significant conformational change was observed in the loop regions. Specifically, the L5 loop is slightly longer, as compared to those of other known proteins, and the flexibility of this loop may facilitate the interaction with double stranded DNA. In addition, we showed that Ape10b2 binds to 16 and 39 bp duplex DNAs with high affinity. On the basis of our analyses, we have created a putative protein-DNA complex model. |
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Keywords: | Ape10b2 Alba Sso10b Sac10b DNA‐binding archaea crystal structure |
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